TY  - JOUR
AU  - Jovčić, Branko
AU  - Venturi, Vittorio
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/534
UR  - http://intor.torlakinstitut.com/handle/123456789/827
AB  - Pseudomonas sp. strain ATCC19151 is a natural isolate from sewage with the ability to degrade detergents. Genes encoding potential choline sulfatase (betC), substrate-binding ABC transporter protein (betD), sulfate transporter (betE), and divergent putative transcriptional regulator (betR) were cloned and characterized from strain ATCC19151. In silico analysis revealed that (1) the BetC protein belongs to alkPPc superfamily and shares CXPXR sequence with the cysteine sulfatases of group I, (2) BetR belongs to the LysR family of transcriptional regulators, (3) BetD is part of the PBPb superfamily of periplasmic and membrane-associated proteins, and (4) BetE is a permease and contains STAS domain. Insertional mutagenesis and genetic complementation show that betC gene encodes a functional choline sulfatase. Analysis of the betC (P (betC) ) and betR (P (betR) ) promoters revealed that they are inducible. BetR activates betC and betR transcription in the presence of choline sulfate, whilst in the absence of choline sulfate, BetR represses its own transcription. It was further established that BetR directly binds to betC-betR intergenic region in vitro, with higher affinity in the presence of choline sulfate as cofactor. Transcription of betC and betR was not induced in the presence of high concentration of NaCl.
PB  - Springer, New York
T2  - Archives of Microbiology
T1  - Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151
EP  - 405
IS  - 6
SP  - 399
VL  - 193
DO  - 10.1007/s00203-011-0685-x
ER  - 

@article{
author = "Jovčić, Branko and Venturi, Vittorio and Topisirović, Ljubiša and Kojić, Milan",
year = "2011",
abstract = "Pseudomonas sp. strain ATCC19151 is a natural isolate from sewage with the ability to degrade detergents. Genes encoding potential choline sulfatase (betC), substrate-binding ABC transporter protein (betD), sulfate transporter (betE), and divergent putative transcriptional regulator (betR) were cloned and characterized from strain ATCC19151. In silico analysis revealed that (1) the BetC protein belongs to alkPPc superfamily and shares CXPXR sequence with the cysteine sulfatases of group I, (2) BetR belongs to the LysR family of transcriptional regulators, (3) BetD is part of the PBPb superfamily of periplasmic and membrane-associated proteins, and (4) BetE is a permease and contains STAS domain. Insertional mutagenesis and genetic complementation show that betC gene encodes a functional choline sulfatase. Analysis of the betC (P (betC) ) and betR (P (betR) ) promoters revealed that they are inducible. BetR activates betC and betR transcription in the presence of choline sulfate, whilst in the absence of choline sulfate, BetR represses its own transcription. It was further established that BetR directly binds to betC-betR intergenic region in vitro, with higher affinity in the presence of choline sulfate as cofactor. Transcription of betC and betR was not induced in the presence of high concentration of NaCl.",
publisher = "Springer, New York",
journal = "Archives of Microbiology",
title = "Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151",
pages = "405-399",
number = "6",
volume = "193",
doi = "10.1007/s00203-011-0685-x"
}

Jovčić, B., Venturi, V., Topisirović, L.,& Kojić, M.. (2011). Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151. in Archives of Microbiology
Springer, New York., 193(6), 399-405.
https://doi.org/10.1007/s00203-011-0685-x

Jovčić B, Venturi V, Topisirović L, Kojić M. Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151. in Archives of Microbiology. 2011;193(6):399-405.
doi:10.1007/s00203-011-0685-x .

Jovčić, Branko, Venturi, Vittorio, Topisirović, Ljubiša, Kojić, Milan, "Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151" in Archives of Microbiology, 193, no. 6 (2011):399-405,
https://doi.org/10.1007/s00203-011-0685-x . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Vasiljević, Zorica
AU  - Đukić, Slobodanka
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/541
UR  - http://intor.torlakinstitut.com/handle/123456789/735
AB  - Molecular detection and surveillance of theresistance genes harboured byPseudomonas aeruginosa are becomingincreasingly important in assessing andcontrolling spread and colonization inhospitals, and in guiding the antibiotictreatment of infections. Metallo-blactamase (MBL)-producing P. aeruginosastrains are slowly but steadily increasingwithin hospitals, causing outbreaks and/orhyperendemic situations in some centres,mostly in the Far East and the south ofEurope (Queenan & Bush, 2007). Theglobal dissemination of MBL-producingP. aeruginosa strains has also reached theBalkan region (Lepsanovic et al., 2008;Sardelic et al., 2003). The objective of ourstudy was to detect and characterize P.aeruginosa isolates producing MBLs fromthe 400-bed paediatric tertiary carehospital Mother and Child Health Instituteof Serbia ‘Dr Vukan Cupic’
PB  - Soc General Microbiology, Reading
T2  - Journal of Medical Microbiology
T1  - Emergence of VIM-2 metallo-beta-lactamase-producing Pseudomonas aeruginosa isolates in a paediatric hospital in Serbia
EP  - 869
IS  - 6
SP  - 868
VL  - 60
DO  - 10.1099/jmm.0.029173-0
ER  - 

@article{
author = "Jovčić, Branko and Vasiljević, Zorica and Đukić, Slobodanka and Topisirović, Ljubiša and Kojić, Milan",
year = "2011",
abstract = "Molecular detection and surveillance of theresistance genes harboured byPseudomonas aeruginosa are becomingincreasingly important in assessing andcontrolling spread and colonization inhospitals, and in guiding the antibiotictreatment of infections. Metallo-blactamase (MBL)-producing P. aeruginosastrains are slowly but steadily increasingwithin hospitals, causing outbreaks and/orhyperendemic situations in some centres,mostly in the Far East and the south ofEurope (Queenan & Bush, 2007). Theglobal dissemination of MBL-producingP. aeruginosa strains has also reached theBalkan region (Lepsanovic et al., 2008;Sardelic et al., 2003). The objective of ourstudy was to detect and characterize P.aeruginosa isolates producing MBLs fromthe 400-bed paediatric tertiary carehospital Mother and Child Health Instituteof Serbia ‘Dr Vukan Cupic’",
publisher = "Soc General Microbiology, Reading",
journal = "Journal of Medical Microbiology",
title = "Emergence of VIM-2 metallo-beta-lactamase-producing Pseudomonas aeruginosa isolates in a paediatric hospital in Serbia",
pages = "869-868",
number = "6",
volume = "60",
doi = "10.1099/jmm.0.029173-0"
}

Jovčić, B., Vasiljević, Z., Đukić, S., Topisirović, L.,& Kojić, M.. (2011). Emergence of VIM-2 metallo-beta-lactamase-producing Pseudomonas aeruginosa isolates in a paediatric hospital in Serbia. in Journal of Medical Microbiology
Soc General Microbiology, Reading., 60(6), 868-869.
https://doi.org/10.1099/jmm.0.029173-0

Jovčić B, Vasiljević Z, Đukić S, Topisirović L, Kojić M. Emergence of VIM-2 metallo-beta-lactamase-producing Pseudomonas aeruginosa isolates in a paediatric hospital in Serbia. in Journal of Medical Microbiology. 2011;60(6):868-869.
doi:10.1099/jmm.0.029173-0 .

Jovčić, Branko, Vasiljević, Zorica, Đukić, Slobodanka, Topisirović, Ljubiša, Kojić, Milan, "Emergence of VIM-2 metallo-beta-lactamase-producing Pseudomonas aeruginosa isolates in a paediatric hospital in Serbia" in Journal of Medical Microbiology, 60, no. 6 (2011):868-869,
https://doi.org/10.1099/jmm.0.029173-0 . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Venturi, V.
AU  - Davison, J.
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/822
AB  - Aims: The presented study was aimed to reveal transcriptional regulation of genes involved in SDS degradation (sdsA and sdsB) in Pseudomonas sp. ATCC19151. In addition, the ability of Pseudomonas sp. ATCC19151 to degrade anionic surfactants present in commercial detergent and septic tank drain was analysed. Methods and Results: Strain ATCC19151, at 30 degrees C, degrades all SDS present in the liquid medium (up to 4% w/v of SDS) within 48 h. ATCC19151 grows in the presence up to 15% (v/v) 'Fairy' commercial detergent and mineralizes 35% of present anionic surfactants. Analysis of the sdsA (P(sdsA)) and divergent sdsB (P(sdsB)) gene promoter activities revealed that SdsB acts as a positive regulator of sdsA and sdsB transcription. P(sdsA) and P(sdsB) activities rose significantly in the presence of the SDS, indicating inducibility of sdsA and sdsB transcription. DNA-binding assay indicated that SdsB directly regulates the transcription of sdsA and sdsB genes. Strain ATCC19151 grew in a sterile septic tank drain and on commercial detergent as sole source of carbon. Conclusions: SdsA enables Pseudomonas sp. ATCC19151 to utilize SDS as a sole carbon source. SdsB is positive transcriptional regulator of sdsA and sdsB genes. Significance and Impact of the Study: Ability of ATCC19151 to degrade anionic surfactants makes Pseudomonas sp. ATCC19151 a good candidate for bioremediation.
PB  - Wiley-Blackwell, Malden
T2  - Journal of Applied Microbiology
T1  - Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants
EP  - 1083
IS  - 3
SP  - 1076
VL  - 109
DO  - 10.1111/j.1365-2672.2010.04738.x
ER  - 

@article{
author = "Jovčić, Branko and Venturi, V. and Davison, J. and Topisirović, Ljubiša and Kojić, Milan",
year = "2010",
abstract = "Aims: The presented study was aimed to reveal transcriptional regulation of genes involved in SDS degradation (sdsA and sdsB) in Pseudomonas sp. ATCC19151. In addition, the ability of Pseudomonas sp. ATCC19151 to degrade anionic surfactants present in commercial detergent and septic tank drain was analysed. Methods and Results: Strain ATCC19151, at 30 degrees C, degrades all SDS present in the liquid medium (up to 4% w/v of SDS) within 48 h. ATCC19151 grows in the presence up to 15% (v/v) 'Fairy' commercial detergent and mineralizes 35% of present anionic surfactants. Analysis of the sdsA (P(sdsA)) and divergent sdsB (P(sdsB)) gene promoter activities revealed that SdsB acts as a positive regulator of sdsA and sdsB transcription. P(sdsA) and P(sdsB) activities rose significantly in the presence of the SDS, indicating inducibility of sdsA and sdsB transcription. DNA-binding assay indicated that SdsB directly regulates the transcription of sdsA and sdsB genes. Strain ATCC19151 grew in a sterile septic tank drain and on commercial detergent as sole source of carbon. Conclusions: SdsA enables Pseudomonas sp. ATCC19151 to utilize SDS as a sole carbon source. SdsB is positive transcriptional regulator of sdsA and sdsB genes. Significance and Impact of the Study: Ability of ATCC19151 to degrade anionic surfactants makes Pseudomonas sp. ATCC19151 a good candidate for bioremediation.",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of Applied Microbiology",
title = "Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants",
pages = "1083-1076",
number = "3",
volume = "109",
doi = "10.1111/j.1365-2672.2010.04738.x"
}

Jovčić, B., Venturi, V., Davison, J., Topisirović, L.,& Kojić, M.. (2010). Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants. in Journal of Applied Microbiology
Wiley-Blackwell, Malden., 109(3), 1076-1083.
https://doi.org/10.1111/j.1365-2672.2010.04738.x

Jovčić B, Venturi V, Davison J, Topisirović L, Kojić M. Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants. in Journal of Applied Microbiology. 2010;109(3):1076-1083.
doi:10.1111/j.1365-2672.2010.04738.x .

Jovčić, Branko, Venturi, V., Davison, J., Topisirović, Ljubiša, Kojić, Milan, "Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants" in Journal of Applied Microbiology, 109, no. 3 (2010):1076-1083,
https://doi.org/10.1111/j.1365-2672.2010.04738.x . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Kojić, Milan
AU  - Tolinački, Maja
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/465
UR  - http://intor.torlakinstitut.com/handle/123456789/825
AB  - Aims: The study of proteolytic activity and examination of proteinase gene region organization in proteolytically active Lactobacillus plantarum strains from different natural sources. Methods and Results: A set of 37 lactobacilli was distinguished by using multiplex PCR assay. Results showed that 34 strains were Lact. plantarum and three of them were Lact. paraplantarum. The examination of proteolytic activity revealed that 28 Lact. plantarum and two Lact. paraplantarum hydrolyse beta-casein. Further analyses of all proteolytically active Lact. plantarum with primers specific for different types of CEPs demonstrated that strain BGSJ3-18 has prtP catalytic domain as well as prtP-prtM intergenic region showing more than 95% sequence identity with the same regions present in Lact. paracasei, Lact. casei and L. lactis. No presence of prtB, prtH or prtR proteinase genes was detected in any of tested Lact. plantarum strains. Conclusions: One out of 28 analysed Lact. plantarum strains harbours the prtP-like gene. The other proteolytically active Lact. plantarum probably possesses a different type of extracellular proteinase(s). Significance and Impact of the Study: It is the first report about the presence of the prtP-like gene in Lact. plantarum, which illustrates the mobility of this gene and its presence in different species.
PB  - Wiley, Hoboken
T2  - Letters in Applied Microbiology
T1  - The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18
EP  - 49
IS  - 1
SP  - 43
VL  - 50
DO  - 10.1111/j.1472-765X.2009.02748.x
ER  - 

@article{
author = "Strahinić, Ivana and Kojić, Milan and Tolinački, Maja and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "Aims: The study of proteolytic activity and examination of proteinase gene region organization in proteolytically active Lactobacillus plantarum strains from different natural sources. Methods and Results: A set of 37 lactobacilli was distinguished by using multiplex PCR assay. Results showed that 34 strains were Lact. plantarum and three of them were Lact. paraplantarum. The examination of proteolytic activity revealed that 28 Lact. plantarum and two Lact. paraplantarum hydrolyse beta-casein. Further analyses of all proteolytically active Lact. plantarum with primers specific for different types of CEPs demonstrated that strain BGSJ3-18 has prtP catalytic domain as well as prtP-prtM intergenic region showing more than 95% sequence identity with the same regions present in Lact. paracasei, Lact. casei and L. lactis. No presence of prtB, prtH or prtR proteinase genes was detected in any of tested Lact. plantarum strains. Conclusions: One out of 28 analysed Lact. plantarum strains harbours the prtP-like gene. The other proteolytically active Lact. plantarum probably possesses a different type of extracellular proteinase(s). Significance and Impact of the Study: It is the first report about the presence of the prtP-like gene in Lact. plantarum, which illustrates the mobility of this gene and its presence in different species.",
publisher = "Wiley, Hoboken",
journal = "Letters in Applied Microbiology",
title = "The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18",
pages = "49-43",
number = "1",
volume = "50",
doi = "10.1111/j.1472-765X.2009.02748.x"
}

Strahinić, I., Kojić, M., Tolinački, M., Fira, Đ.,& Topisirović, L.. (2010). The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18. in Letters in Applied Microbiology
Wiley, Hoboken., 50(1), 43-49.
https://doi.org/10.1111/j.1472-765X.2009.02748.x

Strahinić I, Kojić M, Tolinački M, Fira Đ, Topisirović L. The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18. in Letters in Applied Microbiology. 2010;50(1):43-49.
doi:10.1111/j.1472-765X.2009.02748.x .

Strahinić, Ivana, Kojić, Milan, Tolinački, Maja, Fira, Đorđe, Topisirović, Ljubiša, "The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18" in Letters in Applied Microbiology, 50, no. 1 (2010):43-49,
https://doi.org/10.1111/j.1472-765X.2009.02748.x . .

TY  - JOUR
AU  - Živković, Milica
AU  - Jovčić, Branko
AU  - Kojić, Milan
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/442
UR  - http://intor.torlakinstitut.com/handle/123456789/826
AB  - Ten lactobacilli and one leuconostoc showing auto-aggregation ability were isolated from artisanal cheeses. Furthermore, non-aggregation strains were isolated from the same cheese sample, if existed. The analysis of factor(s) possibly involved in auto-aggregation was performed. The pretreatment of cells with proteinase K resulted in the disappearance of auto-aggregation ability. Moreover, cells also lost aggregation ability after three-times, successive washing in distilled water. Testing the ability of strain Lactobacillus paracasei subsp. paracasei BGSJ2-8 and its aggregation-deficient derivative BGSJ2-81 to co-aggregate with Listeria innocua ATCC33090, Escherichia coli ATCC25922 or Salmonella typhimurium TR251 showed that strain BGSJ2-8 co-aggregated with these strains, but derivative BGSJ2-81 was not. However, the treatment of L. paracasei subsp. paracasei BGSJ2-8 with proteinase K prior to co-aggregation tests resulted in losing co-aggregation ability. Surface properties of selected strains were analyzed by MATS (microbial adhesion to solvents) method. It was noticed that the strains with auto-aggregation ability were highly hydrophobic in comparison with aggregation-deficient ones. Comparative analyses of the surface features of strain L. paracasei subsp. paracasei BGSJ2-8 and its derivative BGSJ2-81 revealed notable difference.
PB  - Springer, New York
T2  - European Food Research and Technology
T1  - Surface properties of Lactobacillus and Leuconostoc isolates from homemade cheeses showing auto-aggregation ability
EP  - 931
IS  - 6
SP  - 925
VL  - 231
DO  - 10.1007/s00217-010-1344-1
ER  - 

@article{
author = "Živković, Milica and Jovčić, Branko and Kojić, Milan and Topisirović, Ljubiša",
year = "2010",
abstract = "Ten lactobacilli and one leuconostoc showing auto-aggregation ability were isolated from artisanal cheeses. Furthermore, non-aggregation strains were isolated from the same cheese sample, if existed. The analysis of factor(s) possibly involved in auto-aggregation was performed. The pretreatment of cells with proteinase K resulted in the disappearance of auto-aggregation ability. Moreover, cells also lost aggregation ability after three-times, successive washing in distilled water. Testing the ability of strain Lactobacillus paracasei subsp. paracasei BGSJ2-8 and its aggregation-deficient derivative BGSJ2-81 to co-aggregate with Listeria innocua ATCC33090, Escherichia coli ATCC25922 or Salmonella typhimurium TR251 showed that strain BGSJ2-8 co-aggregated with these strains, but derivative BGSJ2-81 was not. However, the treatment of L. paracasei subsp. paracasei BGSJ2-8 with proteinase K prior to co-aggregation tests resulted in losing co-aggregation ability. Surface properties of selected strains were analyzed by MATS (microbial adhesion to solvents) method. It was noticed that the strains with auto-aggregation ability were highly hydrophobic in comparison with aggregation-deficient ones. Comparative analyses of the surface features of strain L. paracasei subsp. paracasei BGSJ2-8 and its derivative BGSJ2-81 revealed notable difference.",
publisher = "Springer, New York",
journal = "European Food Research and Technology",
title = "Surface properties of Lactobacillus and Leuconostoc isolates from homemade cheeses showing auto-aggregation ability",
pages = "931-925",
number = "6",
volume = "231",
doi = "10.1007/s00217-010-1344-1"
}

Živković, M., Jovčić, B., Kojić, M.,& Topisirović, L.. (2010). Surface properties of Lactobacillus and Leuconostoc isolates from homemade cheeses showing auto-aggregation ability. in European Food Research and Technology
Springer, New York., 231(6), 925-931.
https://doi.org/10.1007/s00217-010-1344-1

Živković M, Jovčić B, Kojić M, Topisirović L. Surface properties of Lactobacillus and Leuconostoc isolates from homemade cheeses showing auto-aggregation ability. in European Food Research and Technology. 2010;231(6):925-931.
doi:10.1007/s00217-010-1344-1 .

Živković, Milica, Jovčić, Branko, Kojić, Milan, Topisirović, Ljubiša, "Surface properties of Lactobacillus and Leuconostoc isolates from homemade cheeses showing auto-aggregation ability" in European Food Research and Technology, 231, no. 6 (2010):925-931,
https://doi.org/10.1007/s00217-010-1344-1 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Jovčić, Branko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/432
UR  - http://intor.torlakinstitut.com/handle/123456789/727
AB  - A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli. Lactobacillus and Lactococcus strains. It showed high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L paracasei subsp. paracasei BGSJ2-8 was cloned into pA13 using BamHI to obtain the construct, pB5. Sequencing and in silico analysis of pB5 revealed fifteen open reading frames (ORF). Plasmid pSJ2-8 harbours genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. Combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled determination of the primary structure of bacteriocin BacSJ. The bacSJ2-8 gene encodes 68-amino-acid peptide with a double-glycine leader peptide consisting of 18 amino acids, followed by the orf2 (bacSJ2-8i) which encodes the immunity protein of BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirements for production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to class II bacteriocins.
PB  - Elsevier, Amsterdam
T2  - International Journal of Food Microbiology
T1  - Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8
EP  - 124
IS  - 2-3
SP  - 117
VL  - 140
DO  - 10.1016/j.ijfoodmicro.2010.04.010
ER  - 

@article{
author = "Kojić, Milan and Lozo, Jelena and Jovčić, Branko and Strahinić, Ivana and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli. Lactobacillus and Lactococcus strains. It showed high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L paracasei subsp. paracasei BGSJ2-8 was cloned into pA13 using BamHI to obtain the construct, pB5. Sequencing and in silico analysis of pB5 revealed fifteen open reading frames (ORF). Plasmid pSJ2-8 harbours genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. Combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled determination of the primary structure of bacteriocin BacSJ. The bacSJ2-8 gene encodes 68-amino-acid peptide with a double-glycine leader peptide consisting of 18 amino acids, followed by the orf2 (bacSJ2-8i) which encodes the immunity protein of BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirements for production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to class II bacteriocins.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Food Microbiology",
title = "Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8",
pages = "124-117",
number = "2-3",
volume = "140",
doi = "10.1016/j.ijfoodmicro.2010.04.010"
}

Kojić, M., Lozo, J., Jovčić, B., Strahinić, I., Fira, Đ.,& Topisirović, L.. (2010). Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8. in International Journal of Food Microbiology
Elsevier, Amsterdam., 140(2-3), 117-124.
https://doi.org/10.1016/j.ijfoodmicro.2010.04.010

Kojić M, Lozo J, Jovčić B, Strahinić I, Fira Đ, Topisirović L. Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8. in International Journal of Food Microbiology. 2010;140(2-3):117-124.
doi:10.1016/j.ijfoodmicro.2010.04.010 .

Kojić, Milan, Lozo, Jelena, Jovčić, Branko, Strahinić, Ivana, Fira, Đorđe, Topisirović, Ljubiša, "Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8" in International Journal of Food Microbiology, 140, no. 2-3 (2010):117-124,
https://doi.org/10.1016/j.ijfoodmicro.2010.04.010 . .

TY  - JOUR
AU  - Tolinački, Maja
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Terzić-Vidojević, Amarela
AU  - Topisirović, Ljubiša
AU  - Fira, Đorđe
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/719
AB  - The strain Lactobacillus paracasei subsp. paracasei BGUB9 that was isolated from traditionally homemade hard cheese produces bacteriocin designated as BacUB9, with an approximate molecular mass of 4 kDa. Biochemical characterization and the antimicrobial activity test of BacUB9 were performed. The onset of BacUB9 biosynthesis was observed at the end of an exponential phase of growth. Bacteriocin UB9 retained the antimicrobial activity within the pH range from 1 to 10 and after treatment at 100oC for 30 min. The bacteriocin is susceptible to the activity of proteolytic enzymes. Bacteriocin BacUB9 has a very narrow antimicrobial spectrum, limited to several strains that belong to closely related species. The effect of BGUB9 on the growth of the strain Lactobacillus paracasei subsp. paracasei BGHN14 in a mixed culture was monitored. The mode of action of BacUB9 on the strain BGHN14 was identified as bacteriostatic. Plasmid curing results indicated that a plasmid, designated as pUB9, seemed to be responsible for both bacteriocin BacUB9 production and host immunity.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9
EP  - 899
IS  - 4
SP  - 889
VL  - 62
DO  - 10.2298/ABS1004889T
ER  - 

@article{
author = "Tolinački, Maja and Kojić, Milan and Lozo, Jelena and Terzić-Vidojević, Amarela and Topisirović, Ljubiša and Fira, Đorđe",
year = "2010",
abstract = "The strain Lactobacillus paracasei subsp. paracasei BGUB9 that was isolated from traditionally homemade hard cheese produces bacteriocin designated as BacUB9, with an approximate molecular mass of 4 kDa. Biochemical characterization and the antimicrobial activity test of BacUB9 were performed. The onset of BacUB9 biosynthesis was observed at the end of an exponential phase of growth. Bacteriocin UB9 retained the antimicrobial activity within the pH range from 1 to 10 and after treatment at 100oC for 30 min. The bacteriocin is susceptible to the activity of proteolytic enzymes. Bacteriocin BacUB9 has a very narrow antimicrobial spectrum, limited to several strains that belong to closely related species. The effect of BGUB9 on the growth of the strain Lactobacillus paracasei subsp. paracasei BGHN14 in a mixed culture was monitored. The mode of action of BacUB9 on the strain BGHN14 was identified as bacteriostatic. Plasmid curing results indicated that a plasmid, designated as pUB9, seemed to be responsible for both bacteriocin BacUB9 production and host immunity.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9",
pages = "899-889",
number = "4",
volume = "62",
doi = "10.2298/ABS1004889T"
}

Tolinački, M., Kojić, M., Lozo, J., Terzić-Vidojević, A., Topisirović, L.,& Fira, Đ.. (2010). Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(4), 889-899.
https://doi.org/10.2298/ABS1004889T

Tolinački M, Kojić M, Lozo J, Terzić-Vidojević A, Topisirović L, Fira Đ. Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9. in Archives of Biological Sciences. 2010;62(4):889-899.
doi:10.2298/ABS1004889T .

Tolinački, Maja, Kojić, Milan, Lozo, Jelena, Terzić-Vidojević, Amarela, Topisirović, Ljubiša, Fira, Đorđe, "Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9" in Archives of Biological Sciences, 62, no. 4 (2010):889-899,
https://doi.org/10.2298/ABS1004889T . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Jovčić, Branko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/421
UR  - http://intor.torlakinstitut.com/handle/123456789/680
AB  - The aim of this paper was to research the molecular cloning of genes encoding the novel bacteriocin BacSJ from Lactobacillus paracasei subsp. paracasei BGSJ2-8 by using a newly constructed shuttle cloning vector pA13. A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli, Lactobacillus and Lactococcus strains, showing a high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L. paracasei subsp. paracasei BGSJ2-8 was cloned in the pA13 using BamHI, obtaining the construct pB5. Sequencing and in silico analysis of the pB5 revealed 15 open reading frames (ORF). Plasmid pSJ2-8 harbors the genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. The combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled the determination of the primary structure of a bacteriocin BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirement for the production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to the class II bacteriocins. The shuttle cloning vector pA13 could be used as a tool for genetic manipulations in lactobacilli and lactococci.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912
EP  - 243
IS  - 2
SP  - 231
VL  - 62
DO  - 10.2298/ABS1002231K
ER  - 

@article{
author = "Kojić, Milan and Lozo, Jelena and Jovčić, Branko and Strahinić, Ivana and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "The aim of this paper was to research the molecular cloning of genes encoding the novel bacteriocin BacSJ from Lactobacillus paracasei subsp. paracasei BGSJ2-8 by using a newly constructed shuttle cloning vector pA13. A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli, Lactobacillus and Lactococcus strains, showing a high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L. paracasei subsp. paracasei BGSJ2-8 was cloned in the pA13 using BamHI, obtaining the construct pB5. Sequencing and in silico analysis of the pB5 revealed 15 open reading frames (ORF). Plasmid pSJ2-8 harbors the genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. The combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled the determination of the primary structure of a bacteriocin BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirement for the production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to the class II bacteriocins. The shuttle cloning vector pA13 could be used as a tool for genetic manipulations in lactobacilli and lactococci.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912",
pages = "243-231",
number = "2",
volume = "62",
doi = "10.2298/ABS1002231K"
}

Kojić, M., Lozo, J., Jovčić, B., Strahinić, I., Fira, Đ.,& Topisirović, L.. (2010). A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(2), 231-243.
https://doi.org/10.2298/ABS1002231K

Kojić M, Lozo J, Jovčić B, Strahinić I, Fira Đ, Topisirović L. A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912. in Archives of Biological Sciences. 2010;62(2):231-243.
doi:10.2298/ABS1002231K .

Kojić, Milan, Lozo, Jelena, Jovčić, Branko, Strahinić, Ivana, Fira, Đorđe, Topisirović, Ljubiša, "A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912" in Archives of Biological Sciences, 62, no. 2 (2010):231-243,
https://doi.org/10.2298/ABS1002231K . .

TY  - JOUR
AU  - Sanchez Valenzuela, Antonio
AU  - ben Omar, Nabil
AU  - Abriouel, Hikmate
AU  - Lucas Lopez, Rosario
AU  - Veljović, Katarina
AU  - Martinez Canamero, Magdalena
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/820
AB  - A collection of 25 isolates from foods of animal origin (including mainly milk and cheese, together with meat and ham) was studied. Enterococci were identified at species levels as E. faecalis (9 isolates) and E. faecium (16 isolates). Investigation of virulence factors by PCR amplification revealed incomplete sets of cytolysin genes both in E faecalis and E. faecium isolates. Among E. faecalis, PCR amplification revealed a high incidence of genes encoding for enterococcal surface protein esp (7/9 isolates), enterococcal antigen efaA(fs) (6/9), aggregation substance agg (2/9) and sex-pheromone encoding genes ccf, cob, cpd (which were detected in 9, 5 and 3 out of 9 isolates, respectively). By contrast, only esp (7/16 isolates) and efaA(fm) (10/16) were detected among E.faecium. Antibiotic resistance detected at higher frequencies included rifampicin, nitrofurantoin, ciprofloxacin and levofloxacin. Vancomycin resistance was also detected among E.faecalis and E.faecium. E.faecalis isolates showed decarboxylating activity mostly for tyrosine (5/9 isolates), while E faecium isolates showed a broader decarboxylating capacity, involving tyrosine (11/16 isolates) ornithine (6/16), lysine (4/16) and histidine (3/16). Six isolates produced bacteriocins, and genes encoding for enterocins A, B, P, L50, and 1071 were detected. Many isolates tested positive for several of the traits investigated, which raises concerns about their possible role as reservoirs for dissemination of antibiotic resistance and virulence traits in foods.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Control
T1  - Virulence factors, antibiotic resistance, and bacteriocins in enterococci from artisan foods of animal origin
EP  - 385
IS  - 4
SP  - 381
VL  - 20
DO  - 10.1016/j.foodcont.2008.06.004
ER  - 

@article{
author = "Sanchez Valenzuela, Antonio and ben Omar, Nabil and Abriouel, Hikmate and Lucas Lopez, Rosario and Veljović, Katarina and Martinez Canamero, Magdalena and Topisirović, Ljubiša and Kojić, Milan",
year = "2009",
abstract = "A collection of 25 isolates from foods of animal origin (including mainly milk and cheese, together with meat and ham) was studied. Enterococci were identified at species levels as E. faecalis (9 isolates) and E. faecium (16 isolates). Investigation of virulence factors by PCR amplification revealed incomplete sets of cytolysin genes both in E faecalis and E. faecium isolates. Among E. faecalis, PCR amplification revealed a high incidence of genes encoding for enterococcal surface protein esp (7/9 isolates), enterococcal antigen efaA(fs) (6/9), aggregation substance agg (2/9) and sex-pheromone encoding genes ccf, cob, cpd (which were detected in 9, 5 and 3 out of 9 isolates, respectively). By contrast, only esp (7/16 isolates) and efaA(fm) (10/16) were detected among E.faecium. Antibiotic resistance detected at higher frequencies included rifampicin, nitrofurantoin, ciprofloxacin and levofloxacin. Vancomycin resistance was also detected among E.faecalis and E.faecium. E.faecalis isolates showed decarboxylating activity mostly for tyrosine (5/9 isolates), while E faecium isolates showed a broader decarboxylating capacity, involving tyrosine (11/16 isolates) ornithine (6/16), lysine (4/16) and histidine (3/16). Six isolates produced bacteriocins, and genes encoding for enterocins A, B, P, L50, and 1071 were detected. Many isolates tested positive for several of the traits investigated, which raises concerns about their possible role as reservoirs for dissemination of antibiotic resistance and virulence traits in foods.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Control",
title = "Virulence factors, antibiotic resistance, and bacteriocins in enterococci from artisan foods of animal origin",
pages = "385-381",
number = "4",
volume = "20",
doi = "10.1016/j.foodcont.2008.06.004"
}

Sanchez Valenzuela, A., ben Omar, N., Abriouel, H., Lucas Lopez, R., Veljović, K., Martinez Canamero, M., Topisirović, L.,& Kojić, M.. (2009). Virulence factors, antibiotic resistance, and bacteriocins in enterococci from artisan foods of animal origin. in Food Control
Elsevier Sci Ltd, Oxford., 20(4), 381-385.
https://doi.org/10.1016/j.foodcont.2008.06.004

Sanchez Valenzuela A, ben Omar N, Abriouel H, Lucas Lopez R, Veljović K, Martinez Canamero M, Topisirović L, Kojić M. Virulence factors, antibiotic resistance, and bacteriocins in enterococci from artisan foods of animal origin. in Food Control. 2009;20(4):381-385.
doi:10.1016/j.foodcont.2008.06.004 .

Sanchez Valenzuela, Antonio, ben Omar, Nabil, Abriouel, Hikmate, Lucas Lopez, Rosario, Veljović, Katarina, Martinez Canamero, Magdalena, Topisirović, Ljubiša, Kojić, Milan, "Virulence factors, antibiotic resistance, and bacteriocins in enterococci from artisan foods of animal origin" in Food Control, 20, no. 4 (2009):381-385,
https://doi.org/10.1016/j.foodcont.2008.06.004 . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Kojić, Milan
AU  - Tolinački, Maja
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/821
AB  - Strain Lactococcus lactis subsp. lactis bv. diacetylactis S50 harbours five theta-replicating plasmids (pS6, pS7a, pS7b, pS80 and pS140). The aim of this study was to characterize domains involved in the replication and conjugative mobilization of the small plasmids pS7a and pS7b, which are structurally very similar. Complete nucleotide sequences of pS7a and pS7b were determined by cloning DNA fragments of different sizes into Escherichia coli vectors. Linearized plasmids and four EcoRI fragments of the pS7a and pS7b were cloned into an origin probe vector. Constructed plasmids (pSEV10, pSK10, pISE1a and pISE1b) were able to replicate in the strain L. lactis subsp. cremoris MG1363. In addition, experiments showed that plasmids pS7a and pS7b contained oriT sequences and their conjugative transfer directly depended on the presence of pS80 in donor cells. Plasmids pS7a and pS7b contained typical lactococcal theta replication origin and repB gene that enable them to replicate in the strain L. lactis subsp. cremoris MG1363. Plasmid pS80 plays a key role in the conjugative transfer of small plasmids. Plasmids pS7a and pS7b-based derivatives could be valuable tools for genetic manipulation, studying processes of plasmid maintenance and horizontal gene transfer in lactococci.
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors
EP  - 88
IS  - 1
SP  - 78
VL  - 106
DO  - 10.1111/j.1365-2672.2008.03977.x
ER  - 

@article{
author = "Strahinić, Ivana and Kojić, Milan and Tolinački, Maja and Fira, Đorđe and Topisirović, Ljubiša",
year = "2009",
abstract = "Strain Lactococcus lactis subsp. lactis bv. diacetylactis S50 harbours five theta-replicating plasmids (pS6, pS7a, pS7b, pS80 and pS140). The aim of this study was to characterize domains involved in the replication and conjugative mobilization of the small plasmids pS7a and pS7b, which are structurally very similar. Complete nucleotide sequences of pS7a and pS7b were determined by cloning DNA fragments of different sizes into Escherichia coli vectors. Linearized plasmids and four EcoRI fragments of the pS7a and pS7b were cloned into an origin probe vector. Constructed plasmids (pSEV10, pSK10, pISE1a and pISE1b) were able to replicate in the strain L. lactis subsp. cremoris MG1363. In addition, experiments showed that plasmids pS7a and pS7b contained oriT sequences and their conjugative transfer directly depended on the presence of pS80 in donor cells. Plasmids pS7a and pS7b contained typical lactococcal theta replication origin and repB gene that enable them to replicate in the strain L. lactis subsp. cremoris MG1363. Plasmid pS80 plays a key role in the conjugative transfer of small plasmids. Plasmids pS7a and pS7b-based derivatives could be valuable tools for genetic manipulation, studying processes of plasmid maintenance and horizontal gene transfer in lactococci.",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors",
pages = "88-78",
number = "1",
volume = "106",
doi = "10.1111/j.1365-2672.2008.03977.x"
}

Strahinić, I., Kojić, M., Tolinački, M., Fira, Đ.,& Topisirović, L.. (2009). Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors. in Journal of Applied Microbiology
Wiley, Hoboken., 106(1), 78-88.
https://doi.org/10.1111/j.1365-2672.2008.03977.x

Strahinić I, Kojić M, Tolinački M, Fira Đ, Topisirović L. Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors. in Journal of Applied Microbiology. 2009;106(1):78-88.
doi:10.1111/j.1365-2672.2008.03977.x .

Strahinić, Ivana, Kojić, Milan, Tolinački, Maja, Fira, Đorđe, Topisirović, Ljubiša, "Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors" in Journal of Applied Microbiology, 106, no. 1 (2009):78-88,
https://doi.org/10.1111/j.1365-2672.2008.03977.x . .

TY  - JOUR
AU  - Begović, Jelena
AU  - Huys, Geert
AU  - Mayo, Baltasar
AU  - D'Haene, Klaas
AU  - Belen Florez, Ana
AU  - Lozo, Jelena
AU  - Kojić, Milan
AU  - Strahinić, Ivana
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/748
AB  - Little is known about the diversity and distribution of resistance determinants in human commensal bacteria. The aim of this study was to determine the molecular mechanism responsible for high-level erythromycin resistance among five human vaginal Lactobacillus rhamnosus isolates. PCR screening for the presence of ermA, ermB and ermC methylase genes revealed no determinants responsible for detected erythromycin resistance. Therefore, sequences of 23S rRNA genes from L. rhamnosus strains were studied by PCR-RFLP analysis and sequencing of 23S rRNA genes. According to the results, in all erythromycin-resistant L. rhamnosus strains, the presence of a A - gt  G transition mutation at position 2058 was discovered. Additionally, the isolates exhibited heterozygosity for the A2058/G2058 mutation among 23S rRNA gene copies. Presumably, the greatest number of mutated 23S rRNA operons was observed for the L. rhamnosus BGHV1' strain that also had the highest MIC for erythromycin (MIC = 2048 mu g mL(-1)). This study reports the presence of transition mutations in the V region of 23S rRNA genes that most probably account for high-level erythromycin resistance observed for the first time in human vaginal lactobacilli.
PB  - Elsevier, Amsterdam
T2  - Research in Microbiology
T1  - Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance
EP  - 426
IS  - 6
SP  - 421
VL  - 160
DO  - 10.1016/j.resmic.2009.07.005
ER  - 

@article{
author = "Begović, Jelena and Huys, Geert and Mayo, Baltasar and D'Haene, Klaas and Belen Florez, Ana and Lozo, Jelena and Kojić, Milan and Strahinić, Ivana and Topisirović, Ljubiša",
year = "2009",
abstract = "Little is known about the diversity and distribution of resistance determinants in human commensal bacteria. The aim of this study was to determine the molecular mechanism responsible for high-level erythromycin resistance among five human vaginal Lactobacillus rhamnosus isolates. PCR screening for the presence of ermA, ermB and ermC methylase genes revealed no determinants responsible for detected erythromycin resistance. Therefore, sequences of 23S rRNA genes from L. rhamnosus strains were studied by PCR-RFLP analysis and sequencing of 23S rRNA genes. According to the results, in all erythromycin-resistant L. rhamnosus strains, the presence of a A - gt  G transition mutation at position 2058 was discovered. Additionally, the isolates exhibited heterozygosity for the A2058/G2058 mutation among 23S rRNA gene copies. Presumably, the greatest number of mutated 23S rRNA operons was observed for the L. rhamnosus BGHV1' strain that also had the highest MIC for erythromycin (MIC = 2048 mu g mL(-1)). This study reports the presence of transition mutations in the V region of 23S rRNA genes that most probably account for high-level erythromycin resistance observed for the first time in human vaginal lactobacilli.",
publisher = "Elsevier, Amsterdam",
journal = "Research in Microbiology",
title = "Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance",
pages = "426-421",
number = "6",
volume = "160",
doi = "10.1016/j.resmic.2009.07.005"
}

Begović, J., Huys, G., Mayo, B., D'Haene, K., Belen Florez, A., Lozo, J., Kojić, M., Strahinić, I.,& Topisirović, L.. (2009). Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance. in Research in Microbiology
Elsevier, Amsterdam., 160(6), 421-426.
https://doi.org/10.1016/j.resmic.2009.07.005

Begović J, Huys G, Mayo B, D'Haene K, Belen Florez A, Lozo J, Kojić M, Strahinić I, Topisirović L. Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance. in Research in Microbiology. 2009;160(6):421-426.
doi:10.1016/j.resmic.2009.07.005 .

Begović, Jelena, Huys, Geert, Mayo, Baltasar, D'Haene, Klaas, Belen Florez, Ana, Lozo, Jelena, Kojić, Milan, Strahinić, Ivana, Topisirović, Ljubiša, "Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance" in Research in Microbiology, 160, no. 6 (2009):421-426,
https://doi.org/10.1016/j.resmic.2009.07.005 . .

TY  - JOUR
AU  - Begović, Jelena
AU  - Huys, Geert
AU  - Mayo, Baltasar
AU  - D'Haene, Klaas
AU  - Belen Florez, Ana
AU  - Lozo, Jelena
AU  - Kojić, Milan
AU  - Strahinić, Ivana
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/749
AB  - Little is known about the diversity and distribution of resistance determinants in human commensal bacteria. The aim of this study was to determine the molecular mechanism responsible for high-level erythromycin resistance among five human vaginal Lactobacillus rhamnosus isolates. PCR screening for the presence of ermA, ermB and ermC methylase genes revealed no determinants responsible for detected erythromycin resistance. Therefore, sequences of 23S rRNA genes from L. rhamnosus strains were studied by PCR-RFLP analysis and sequencing of 23S rRNA genes. According to the results, in all erythromycin-resistant L. rhamnosus strains, the presence of a A - gt  G transition mutation at position 2058 was discovered. Additionally, the isolates exhibited heterozygosity for the A2058/G2058 mutation among 23S rRNA gene copies. Presumably, the greatest number of mutated 23S rRNA operons was observed for the L. rhamnosus BGHV1' strain that also had the highest MIC for erythromycin (MIC = 2048 mu g mL(-1)). This study reports the presence of transition mutations in the V region of 23S rRNA genes that most probably account for high-level erythromycin resistance observed for the first time in human vaginal lactobacilli.
PB  - Elsevier
T2  - Research in Microbiology
T1  - Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance
EP  - 426
IS  - 6
SP  - 421
VL  - 160
DO  - 10.1016/j.resmic.2009.07.005
ER  - 

@article{
author = "Begović, Jelena and Huys, Geert and Mayo, Baltasar and D'Haene, Klaas and Belen Florez, Ana and Lozo, Jelena and Kojić, Milan and Strahinić, Ivana and Topisirović, Ljubiša",
year = "2009",
abstract = "Little is known about the diversity and distribution of resistance determinants in human commensal bacteria. The aim of this study was to determine the molecular mechanism responsible for high-level erythromycin resistance among five human vaginal Lactobacillus rhamnosus isolates. PCR screening for the presence of ermA, ermB and ermC methylase genes revealed no determinants responsible for detected erythromycin resistance. Therefore, sequences of 23S rRNA genes from L. rhamnosus strains were studied by PCR-RFLP analysis and sequencing of 23S rRNA genes. According to the results, in all erythromycin-resistant L. rhamnosus strains, the presence of a A - gt  G transition mutation at position 2058 was discovered. Additionally, the isolates exhibited heterozygosity for the A2058/G2058 mutation among 23S rRNA gene copies. Presumably, the greatest number of mutated 23S rRNA operons was observed for the L. rhamnosus BGHV1' strain that also had the highest MIC for erythromycin (MIC = 2048 mu g mL(-1)). This study reports the presence of transition mutations in the V region of 23S rRNA genes that most probably account for high-level erythromycin resistance observed for the first time in human vaginal lactobacilli.",
publisher = "Elsevier",
journal = "Research in Microbiology",
title = "Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance",
pages = "426-421",
number = "6",
volume = "160",
doi = "10.1016/j.resmic.2009.07.005"
}

Begović, J., Huys, G., Mayo, B., D'Haene, K., Belen Florez, A., Lozo, J., Kojić, M., Strahinić, I.,& Topisirović, L.. (2009). Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance. in Research in Microbiology
Elsevier., 160(6), 421-426.
https://doi.org/10.1016/j.resmic.2009.07.005

Begović J, Huys G, Mayo B, D'Haene K, Belen Florez A, Lozo J, Kojić M, Strahinić I, Topisirović L. Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance. in Research in Microbiology. 2009;160(6):421-426.
doi:10.1016/j.resmic.2009.07.005 .

Begović, Jelena, Huys, Geert, Mayo, Baltasar, D'Haene, Klaas, Belen Florez, Ana, Lozo, Jelena, Kojić, Milan, Strahinić, Ivana, Topisirović, Ljubiša, "Human vaginal Lactobacillus rhamnosus harbor mutation in 23S rRNA associated with erythromycin resistance" in Research in Microbiology, 160, no. 6 (2009):421-426,
https://doi.org/10.1016/j.resmic.2009.07.005 . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Begović, Jelena
AU  - Lozo, Jelena
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/345
UR  - http://intor.torlakinstitut.com/handle/123456789/730
AB  - Poznato je da soj Pseudomonas sp. ATCC19151 poseduje gen koji kodira Potencijalnu alkilsulfatazu. U ovom radu analizirana je sposobnost rasta ovog soja u minimalnom medijum usa različitim koncentracijama natrijum dodecilsulfata (0.5, 0.75 i 1 %) kao jedinim izvorom ugljenika. Pokazano je da Pseudomonas sp. ATCC19151 ispoljava najbolji rast uminimalnom medijumusa 0.5 % natrijum dodecil sulfata, te je stoga ova koncentracija uzeta kao optimalna za testiranje dinamike korišćenja natrijum dodecil sulfata tokom različitih faza rasta. Dinamika korišćenja natrijum dodecil sulfata podudarala se sa rastom kulture. Pored toga u cilju detaljnije karakterizacije soja, analizirana je i osetljivost Pseudomonas sp. ATCC19151 na antibiotike. Pokazano je da je analizirani soj rezistentan na šest (ampicilin, tetraciklin, hloramfenikol, tobramicin, nalidiksičnukiselinui gentamicin) od devet analiziranih antibiotika.
AB  - Pseudomonas sp. ATCC19151 harbors a gene encoding a putative alkylsulfatase (sdsA). Here we report a growth ability of this strain in minimal media containing 0.5, 0.75, and 1% sodium dodecyl sulfate as the sole carbon source. The most prominent growth was detected for the minimal medium with 0.5% SDS, so this concentration of SDS was used to monitor Pseudomonas sp. ATCC19151 SDS biodegradation dynamics. Bacterial growth coincided with the disappearance of SDS. Antibiotic susceptibility was tested as well. Pseudomonas sp. ATCC19151 was resistant to six out of nine tested antibiotics, including ampicillin, tetracycline, chloramphenicol, tobramycin, nalidixic acid, and gentamycin.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Dinamika korišćenja natrijum dodecil sulfata i osetljivost na antibiotike soja Pseudomonas sp. ATCC19151
T1  - Dynamics of sodium dodecyl sulfate utilization andantibiotic susceptibility of strain Pseudomonas sp. ATCC19151
EP  - 164
IS  - 2
SP  - 159
VL  - 61
DO  - 10.2298/ABS0902159J
ER  - 

@article{
author = "Jovčić, Branko and Begović, Jelena and Lozo, Jelena and Topisirović, Ljubiša and Kojić, Milan",
year = "2009",
abstract = "Poznato je da soj Pseudomonas sp. ATCC19151 poseduje gen koji kodira Potencijalnu alkilsulfatazu. U ovom radu analizirana je sposobnost rasta ovog soja u minimalnom medijum usa različitim koncentracijama natrijum dodecilsulfata (0.5, 0.75 i 1 %) kao jedinim izvorom ugljenika. Pokazano je da Pseudomonas sp. ATCC19151 ispoljava najbolji rast uminimalnom medijumusa 0.5 % natrijum dodecil sulfata, te je stoga ova koncentracija uzeta kao optimalna za testiranje dinamike korišćenja natrijum dodecil sulfata tokom različitih faza rasta. Dinamika korišćenja natrijum dodecil sulfata podudarala se sa rastom kulture. Pored toga u cilju detaljnije karakterizacije soja, analizirana je i osetljivost Pseudomonas sp. ATCC19151 na antibiotike. Pokazano je da je analizirani soj rezistentan na šest (ampicilin, tetraciklin, hloramfenikol, tobramicin, nalidiksičnukiselinui gentamicin) od devet analiziranih antibiotika., Pseudomonas sp. ATCC19151 harbors a gene encoding a putative alkylsulfatase (sdsA). Here we report a growth ability of this strain in minimal media containing 0.5, 0.75, and 1% sodium dodecyl sulfate as the sole carbon source. The most prominent growth was detected for the minimal medium with 0.5% SDS, so this concentration of SDS was used to monitor Pseudomonas sp. ATCC19151 SDS biodegradation dynamics. Bacterial growth coincided with the disappearance of SDS. Antibiotic susceptibility was tested as well. Pseudomonas sp. ATCC19151 was resistant to six out of nine tested antibiotics, including ampicillin, tetracycline, chloramphenicol, tobramycin, nalidixic acid, and gentamycin.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Dinamika korišćenja natrijum dodecil sulfata i osetljivost na antibiotike soja Pseudomonas sp. ATCC19151, Dynamics of sodium dodecyl sulfate utilization andantibiotic susceptibility of strain Pseudomonas sp. ATCC19151",
pages = "164-159",
number = "2",
volume = "61",
doi = "10.2298/ABS0902159J"
}

Jovčić, B., Begović, J., Lozo, J., Topisirović, L.,& Kojić, M.. (2009). Dinamika korišćenja natrijum dodecil sulfata i osetljivost na antibiotike soja Pseudomonas sp. ATCC19151. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 61(2), 159-164.
https://doi.org/10.2298/ABS0902159J

Jovčić B, Begović J, Lozo J, Topisirović L, Kojić M. Dinamika korišćenja natrijum dodecil sulfata i osetljivost na antibiotike soja Pseudomonas sp. ATCC19151. in Archives of Biological Sciences. 2009;61(2):159-164.
doi:10.2298/ABS0902159J .

Jovčić, Branko, Begović, Jelena, Lozo, Jelena, Topisirović, Ljubiša, Kojić, Milan, "Dinamika korišćenja natrijum dodecil sulfata i osetljivost na antibiotike soja Pseudomonas sp. ATCC19151" in Archives of Biological Sciences, 61, no. 2 (2009):159-164,
https://doi.org/10.2298/ABS0902159J . .

TY  - JOUR
AU  - Busarcević, M.
AU  - Kojić, Milan
AU  - Dalgalarrondo, M.
AU  - Chobert, J. -M.
AU  - Haertle, T.
AU  - Topisirović, Ljubiša
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/817
AB  - Introduction: Lactobacillus salivarius BGHO1, a human oral isolate with antagonistic activity against growth of Streptococcus mutans, Streptococcus pneumoniae, Staphylococcus aureus, Enterococcus faecalis, Micrococcus flavus, and Salmonella enteritidis, probably produces more than one proteinaceous antimicrobial substance. The objective of this study was the purification of a bacteriocin, named LS1, produced by L. salivarius BGHO1. Methods: A simple and fast procedure for bacteriocin purification was developed, consisting of reverse-phase chromatography of the ammonium sulfate precipitate of cell-free culture supernatant by fast protein liquid chromatography and high-performance liquid chromatography, followed by tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with the subsequent extraction of bacteriocin from the gel. Results: The supernatant of L. salivarius BGHO1 culture retained its antimicrobial activity after boiling in a water bath for 15 min. Its antimicrobial activity was also maintained even after treatment for 20 min at 121 degrees C in an autoclave. Bacteriocin LS1 was purified to homogeneity. The molecular mass of bacteriocin LS1 was estimated to be approximately 10 kDa, based on tricine SDS-PAGE. During purification, another compound with antimicrobial activity, produced by L. salivarius BGHO1, was detected. The molecular mass of this compound was estimated to be approximately 5 kDa, based on tricine SDS-PAGE. Conclusion: Our results imply that LS1 is most probably a new bacteriocin, different from previously described bacteriocins produced by L. salivarius strains. The purification of bacteriocin LS1 enabled the further characterization of LS1 on both the molecular and genetic levels.
PB  - Wiley, Hoboken
T2  - Oral Microbiology and Immunology
T1  - Purification of bacteriocin LS1 produced by human oral isolate Lactobacillus salivarius BGHO1
EP  - 258
IS  - 3
SP  - 254
VL  - 23
DO  - 10.1111/j.1399-302X.2007.00420.x
ER  - 

@article{
author = "Busarcević, M. and Kojić, Milan and Dalgalarrondo, M. and Chobert, J. -M. and Haertle, T. and Topisirović, Ljubiša",
year = "2008",
abstract = "Introduction: Lactobacillus salivarius BGHO1, a human oral isolate with antagonistic activity against growth of Streptococcus mutans, Streptococcus pneumoniae, Staphylococcus aureus, Enterococcus faecalis, Micrococcus flavus, and Salmonella enteritidis, probably produces more than one proteinaceous antimicrobial substance. The objective of this study was the purification of a bacteriocin, named LS1, produced by L. salivarius BGHO1. Methods: A simple and fast procedure for bacteriocin purification was developed, consisting of reverse-phase chromatography of the ammonium sulfate precipitate of cell-free culture supernatant by fast protein liquid chromatography and high-performance liquid chromatography, followed by tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with the subsequent extraction of bacteriocin from the gel. Results: The supernatant of L. salivarius BGHO1 culture retained its antimicrobial activity after boiling in a water bath for 15 min. Its antimicrobial activity was also maintained even after treatment for 20 min at 121 degrees C in an autoclave. Bacteriocin LS1 was purified to homogeneity. The molecular mass of bacteriocin LS1 was estimated to be approximately 10 kDa, based on tricine SDS-PAGE. During purification, another compound with antimicrobial activity, produced by L. salivarius BGHO1, was detected. The molecular mass of this compound was estimated to be approximately 5 kDa, based on tricine SDS-PAGE. Conclusion: Our results imply that LS1 is most probably a new bacteriocin, different from previously described bacteriocins produced by L. salivarius strains. The purification of bacteriocin LS1 enabled the further characterization of LS1 on both the molecular and genetic levels.",
publisher = "Wiley, Hoboken",
journal = "Oral Microbiology and Immunology",
title = "Purification of bacteriocin LS1 produced by human oral isolate Lactobacillus salivarius BGHO1",
pages = "258-254",
number = "3",
volume = "23",
doi = "10.1111/j.1399-302X.2007.00420.x"
}

Busarcević, M., Kojić, M., Dalgalarrondo, M., Chobert, J. -M., Haertle, T.,& Topisirović, L.. (2008). Purification of bacteriocin LS1 produced by human oral isolate Lactobacillus salivarius BGHO1. in Oral Microbiology and Immunology
Wiley, Hoboken., 23(3), 254-258.
https://doi.org/10.1111/j.1399-302X.2007.00420.x

Busarcević M, Kojić M, Dalgalarrondo M, Chobert J-, Haertle T, Topisirović L. Purification of bacteriocin LS1 produced by human oral isolate Lactobacillus salivarius BGHO1. in Oral Microbiology and Immunology. 2008;23(3):254-258.
doi:10.1111/j.1399-302X.2007.00420.x .

Busarcević, M., Kojić, Milan, Dalgalarrondo, M., Chobert, J. -M., Haertle, T., Topisirović, Ljubiša, "Purification of bacteriocin LS1 produced by human oral isolate Lactobacillus salivarius BGHO1" in Oral Microbiology and Immunology, 23, no. 3 (2008):254-258,
https://doi.org/10.1111/j.1399-302X.2007.00420.x . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Bertani, Iris
AU  - Venturi, Vittorio
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2008
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/333
UR  - http://intor.torlakinstitut.com/handle/123456789/679
AB  - The sigma(S) subunit of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genes in Gram-negative bacteria. The Pseudomonas putida rpoS gene is transcribed as a monocistronic rpoS mRNA with a 368 nucleotide-long 5' untranslated region (5' UTR). In this study, we investigate the posttranscriptional control of RpoS synthesis using rpoS-lacZ transcriptional and translational fusions consisting of the native promoter and deletions of 5' UTR or insertion into UTR. The differing activity of constructed translational fusions strongly indicated that the 5' UTR is involved in the translational regulation of RpoS expression in the stationary phase. The results obtained herein demonstrated that the structure of UTR performs an important function in the translational regulation of the rpoS gene.
PB  - Microbiology Soc Korea, Seoul
T2  - Journal of Microbiology
T1  - 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation
EP  - 61
IS  - 1
SP  - 56
VL  - 46
DO  - 10.1007/s12275-007-0127-2
ER  - 

@article{
author = "Jovčić, Branko and Bertani, Iris and Venturi, Vittorio and Topisirović, Ljubiša and Kojić, Milan",
year = "2008",
abstract = "The sigma(S) subunit of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genes in Gram-negative bacteria. The Pseudomonas putida rpoS gene is transcribed as a monocistronic rpoS mRNA with a 368 nucleotide-long 5' untranslated region (5' UTR). In this study, we investigate the posttranscriptional control of RpoS synthesis using rpoS-lacZ transcriptional and translational fusions consisting of the native promoter and deletions of 5' UTR or insertion into UTR. The differing activity of constructed translational fusions strongly indicated that the 5' UTR is involved in the translational regulation of RpoS expression in the stationary phase. The results obtained herein demonstrated that the structure of UTR performs an important function in the translational regulation of the rpoS gene.",
publisher = "Microbiology Soc Korea, Seoul",
journal = "Journal of Microbiology",
title = "5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation",
pages = "61-56",
number = "1",
volume = "46",
doi = "10.1007/s12275-007-0127-2"
}

Jovčić, B., Bertani, I., Venturi, V., Topisirović, L.,& Kojić, M.. (2008). 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation. in Journal of Microbiology
Microbiology Soc Korea, Seoul., 46(1), 56-61.
https://doi.org/10.1007/s12275-007-0127-2

Jovčić B, Bertani I, Venturi V, Topisirović L, Kojić M. 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation. in Journal of Microbiology. 2008;46(1):56-61.
doi:10.1007/s12275-007-0127-2 .

Jovčić, Branko, Bertani, Iris, Venturi, Vittorio, Topisirović, Ljubiša, Kojić, Milan, "5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation" in Journal of Microbiology, 46, no. 1 (2008):56-61,
https://doi.org/10.1007/s12275-007-0127-2 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Begović, Jelena
AU  - Jovčić, Branko
AU  - Topisirović, Ljubiša
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/812
AB  - Pet izolata laktokoka proizvođača bakteriocina izolovanih iz kefira pripremljenog na tradicionalan način determinisano je kao Lactococcus lactis subsp. lactis. Analizirani izolati poseduju različite plazmidne profile i među njima nije detektovana uzajamna antimikrobna aktivnost. Takođe prirodni izolat BGKF26 je rezistentan na aktivnost soja NP45, proizvođača nizina. Eksperimenti čišćenja plazmida pokazali su da se geni _a sintezu bakteriocina i proteinaza nalaze na različitim genetičkim elementima, osim kod izolata BGKF26. Sinteza analiziranih bakteriocina zavisi od koncentracije kazitona ili triptona u medijumu. Više koncentracije kazitona ili triptona indukuju bakteriocinsku aktivnost. Hibridizacioni eksperimenti su pokazali da su analizirani bakteriocini najverovatnije slični laktokokcinima.
AB  - Five bacteriocin-producing lactococci isolates from traditionally prepared kefir were determined as Lactococcus lactis subsp. lactis. The analyzed isolates showed different plasmid profiles and no cross inhibition between them was detected. Moreover, natural isolate BGKF26 was resistant to the antimicrobial activity of nisin producing strain NP45. Plasmid curing experiments revealed that the genes encoding bacteriocin and proteinase production are located on separate genetic elements, except in BGKF26. Production of the tested bacteriocins depends on the concentration of casitone or triptone in the medium. Higher concentrations of casitone or triptone induce bacteriocin activity. Our DNA-DNA hybridization analyses suggest that the analyzed antimicrobial compounds probably are lactococcin-like bacteriocins.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Karakterizacija laktokoka izolovanih iz kefira pripremljenog u domaćinstvu
T1  - Characterization of lactococci isolated from homemade kefir
EP  - 22
IS  - 1
SP  - 13
VL  - 59
DO  - 10.2298/ABS0701013K
ER  - 

@article{
author = "Kojić, Milan and Lozo, Jelena and Begović, Jelena and Jovčić, Branko and Topisirović, Ljubiša",
year = "2007",
abstract = "Pet izolata laktokoka proizvođača bakteriocina izolovanih iz kefira pripremljenog na tradicionalan način determinisano je kao Lactococcus lactis subsp. lactis. Analizirani izolati poseduju različite plazmidne profile i među njima nije detektovana uzajamna antimikrobna aktivnost. Takođe prirodni izolat BGKF26 je rezistentan na aktivnost soja NP45, proizvođača nizina. Eksperimenti čišćenja plazmida pokazali su da se geni _a sintezu bakteriocina i proteinaza nalaze na različitim genetičkim elementima, osim kod izolata BGKF26. Sinteza analiziranih bakteriocina zavisi od koncentracije kazitona ili triptona u medijumu. Više koncentracije kazitona ili triptona indukuju bakteriocinsku aktivnost. Hibridizacioni eksperimenti su pokazali da su analizirani bakteriocini najverovatnije slični laktokokcinima., Five bacteriocin-producing lactococci isolates from traditionally prepared kefir were determined as Lactococcus lactis subsp. lactis. The analyzed isolates showed different plasmid profiles and no cross inhibition between them was detected. Moreover, natural isolate BGKF26 was resistant to the antimicrobial activity of nisin producing strain NP45. Plasmid curing experiments revealed that the genes encoding bacteriocin and proteinase production are located on separate genetic elements, except in BGKF26. Production of the tested bacteriocins depends on the concentration of casitone or triptone in the medium. Higher concentrations of casitone or triptone induce bacteriocin activity. Our DNA-DNA hybridization analyses suggest that the analyzed antimicrobial compounds probably are lactococcin-like bacteriocins.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Karakterizacija laktokoka izolovanih iz kefira pripremljenog u domaćinstvu, Characterization of lactococci isolated from homemade kefir",
pages = "22-13",
number = "1",
volume = "59",
doi = "10.2298/ABS0701013K"
}

Kojić, M., Lozo, J., Begović, J., Jovčić, B.,& Topisirović, L.. (2007). Karakterizacija laktokoka izolovanih iz kefira pripremljenog u domaćinstvu. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 59(1), 13-22.
https://doi.org/10.2298/ABS0701013K

Kojić M, Lozo J, Begović J, Jovčić B, Topisirović L. Karakterizacija laktokoka izolovanih iz kefira pripremljenog u domaćinstvu. in Archives of Biological Sciences. 2007;59(1):13-22.
doi:10.2298/ABS0701013K .

Kojić, Milan, Lozo, Jelena, Begović, Jelena, Jovčić, Branko, Topisirović, Ljubiša, "Karakterizacija laktokoka izolovanih iz kefira pripremljenog u domaćinstvu" in Archives of Biological Sciences, 59, no. 1 (2007):13-22,
https://doi.org/10.2298/ABS0701013K . .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Jovčić, Branko
AU  - Kojić, Milan
AU  - Dalgalarrondo, Michele
AU  - Chobert, Jean-Marc
AU  - Haertle, Thomas
AU  - Topisirović, Ljubiša
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/814
AB  - Screening the collection of natural isolates from semi-hard homemade cheese resulted in isolation and characterization of strain Lactobacillus paracasei subsp. paracasei BGSJ2-8. The strain BGSJ2-8 harbors several important phenotypes, such as bacteriocin production, aggregation phenomenon, and production of proteinase. Bacteriocin SJ was purified by three-step chromatography. Mass spectrometry established molecular mass of the active peptide at 5372 Da. The auto - aggregation phenotype of wild-type (WT) strain was mediated by secreted aggregation-promoting factor (protein of molecular mass  gt  200 kDa), probably acting in cooperation with other cell surface protein(s). Comparative study of WT and its spontaneous nonaggregating derivative revealed that aggregation factor was responsible for the observed differences in the bacteriocin and proteinase activities. Bacteriocin SJ activity and resistance to different stresses were higher in the presence of aggregating factor. In contrast, proteinase activity was stronger in the nonaggregating derivative.
PB  - Springer, New York
T2  - Current Microbiology
T1  - Molecular characterization of a novel bacteriocin and an unusually large aggregation factor of Lactobacillus paracasei subsp paracasei BGSJ2-8, a natural isolate from homemade cheese
EP  - 271
IS  - 3
SP  - 266
VL  - 55
DO  - 10.1007/s00284-007-0159-1
ER  - 

@article{
author = "Lozo, Jelena and Jovčić, Branko and Kojić, Milan and Dalgalarrondo, Michele and Chobert, Jean-Marc and Haertle, Thomas and Topisirović, Ljubiša",
year = "2007",
abstract = "Screening the collection of natural isolates from semi-hard homemade cheese resulted in isolation and characterization of strain Lactobacillus paracasei subsp. paracasei BGSJ2-8. The strain BGSJ2-8 harbors several important phenotypes, such as bacteriocin production, aggregation phenomenon, and production of proteinase. Bacteriocin SJ was purified by three-step chromatography. Mass spectrometry established molecular mass of the active peptide at 5372 Da. The auto - aggregation phenotype of wild-type (WT) strain was mediated by secreted aggregation-promoting factor (protein of molecular mass  gt  200 kDa), probably acting in cooperation with other cell surface protein(s). Comparative study of WT and its spontaneous nonaggregating derivative revealed that aggregation factor was responsible for the observed differences in the bacteriocin and proteinase activities. Bacteriocin SJ activity and resistance to different stresses were higher in the presence of aggregating factor. In contrast, proteinase activity was stronger in the nonaggregating derivative.",
publisher = "Springer, New York",
journal = "Current Microbiology",
title = "Molecular characterization of a novel bacteriocin and an unusually large aggregation factor of Lactobacillus paracasei subsp paracasei BGSJ2-8, a natural isolate from homemade cheese",
pages = "271-266",
number = "3",
volume = "55",
doi = "10.1007/s00284-007-0159-1"
}

Lozo, J., Jovčić, B., Kojić, M., Dalgalarrondo, M., Chobert, J., Haertle, T.,& Topisirović, L.. (2007). Molecular characterization of a novel bacteriocin and an unusually large aggregation factor of Lactobacillus paracasei subsp paracasei BGSJ2-8, a natural isolate from homemade cheese. in Current Microbiology
Springer, New York., 55(3), 266-271.
https://doi.org/10.1007/s00284-007-0159-1

Lozo J, Jovčić B, Kojić M, Dalgalarrondo M, Chobert J, Haertle T, Topisirović L. Molecular characterization of a novel bacteriocin and an unusually large aggregation factor of Lactobacillus paracasei subsp paracasei BGSJ2-8, a natural isolate from homemade cheese. in Current Microbiology. 2007;55(3):266-271.
doi:10.1007/s00284-007-0159-1 .

Lozo, Jelena, Jovčić, Branko, Kojić, Milan, Dalgalarrondo, Michele, Chobert, Jean-Marc, Haertle, Thomas, Topisirović, Ljubiša, "Molecular characterization of a novel bacteriocin and an unusually large aggregation factor of Lactobacillus paracasei subsp paracasei BGSJ2-8, a natural isolate from homemade cheese" in Current Microbiology, 55, no. 3 (2007):266-271,
https://doi.org/10.1007/s00284-007-0159-1 . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Cvetanović, D.
AU  - Kojić, Milan
AU  - Fira, Đorđe
AU  - Tolinački, Maja
AU  - Topisirović, Ljubiša
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/815
AB  - Soj Lactococcus lactis subsp. lactis BGSM1-19, izolovan iz sira tradicionalno proizvedenog u domaćinstvu, sintetiše dva bakteriocina: bakteriocin BacSMa koji pripada grupi laktokokcina B i bakteriocin BacSMb koji pokazuje visoku homologiju sa lakticinom RM. Čišćenjem plazmida, sa relativno niskim prinosom (0,33%), dobijene su dve grupe derivata: BacSMa- BacSMas derivat i BacSMa- BacSMas, BacSMb-, BacSMbs.. Sinteza bakteriocina je ispitivana tokom logaritamske faze rasta pri čemu je utvrđen maksimum proizvodnje u kulturi staroj 8 sati gajenoj na temperaturi od 30oC, što odgovara ranoj stacionarnoj fazi rasta. Biohemijska karakterizacija je ukazala da soj BGSM1-19 zadržava antimikrobnu aktivnost u opsegu pH vrednosti od 1 do 12 kao i posle tretmana na 100 oC u trajanju od 15 minuta. Utvrđeno je da se antimikrobna aktivnost potpuno gubi nakon tretmana različitim proteolitičkim enzimima. Soj BGSM1-19 poseduje pet plazmida. U eksperimentima čišćenja od plazmida utvrđeno je da se geni za sintezu i imunost na bakteriocine nalaze na plazmidima. Pored toga, BGSM1-19 pokazuje antimikrobnu aktivnost na ispitivane patogene bakterije kao što su Salmonella paratyphi, Micrococcus flavus, Pseudomonas aeruginosa i Staphylococcus aureus.
AB  - The strain Lactococcus lactis subsp. lactis BGSM1-19, isolated from traditionally homemade white cheese, produces two bacteriocins: lactococcin B-like bacteriocin named bacteriocin BacSMa and bacteriocin BacSMb which have shown similarity with lacticin RM. Plasmid curing resulted in a low yield (0.33%) of BacSMa- BacSMas and BacSMa- BacSMas, BacSMb-, BacSMbs derivatives. The bacteriocin biosynthesis was observed in the logarithmic phase of growth and the production plateau was reached after 8 h of incubation at 30oC, when the culture entered the early stationary phase. Biochemical characterization showed that strain BGSM1-19 retained antimicrobial activity within the pH range of 1 to 12 or after treatment at 100oC for 15 min. However, bacteriocin activity was completely lost after treatment with different proteolytic enzymes. The strain BGSM1-19 contains five plasmids. Plasmid curing indicated that genes coding for bacteriocins synthesis and immunity seem to be located on plasmids. BGSM1-19 exhibited antimicrobial activity against some pathogenic bacteria such as Salmonella paratyphi, Micrococcus flavus, Pseudomonas aeruginosa and Staphylococcus aureus.
PB  - Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd
T2  - Acta Veterinaria-Beograd
T1  - Karakterizacija i antimikrobna aktivnost prirodnog izolata Lactococcus lactis subsp. lactis BGSM1-19
T1  - Characterization and antimicrobial activity of natural isolate Lactococcus lactis subsp. lactis BGSM1-19
EP  - 521
IS  - 5-6
SP  - 509
VL  - 57
DO  - 10.2298/AVB0706509S
ER  - 

@article{
author = "Strahinić, Ivana and Cvetanović, D. and Kojić, Milan and Fira, Đorđe and Tolinački, Maja and Topisirović, Ljubiša",
year = "2007",
abstract = "Soj Lactococcus lactis subsp. lactis BGSM1-19, izolovan iz sira tradicionalno proizvedenog u domaćinstvu, sintetiše dva bakteriocina: bakteriocin BacSMa koji pripada grupi laktokokcina B i bakteriocin BacSMb koji pokazuje visoku homologiju sa lakticinom RM. Čišćenjem plazmida, sa relativno niskim prinosom (0,33%), dobijene su dve grupe derivata: BacSMa- BacSMas derivat i BacSMa- BacSMas, BacSMb-, BacSMbs.. Sinteza bakteriocina je ispitivana tokom logaritamske faze rasta pri čemu je utvrđen maksimum proizvodnje u kulturi staroj 8 sati gajenoj na temperaturi od 30oC, što odgovara ranoj stacionarnoj fazi rasta. Biohemijska karakterizacija je ukazala da soj BGSM1-19 zadržava antimikrobnu aktivnost u opsegu pH vrednosti od 1 do 12 kao i posle tretmana na 100 oC u trajanju od 15 minuta. Utvrđeno je da se antimikrobna aktivnost potpuno gubi nakon tretmana različitim proteolitičkim enzimima. Soj BGSM1-19 poseduje pet plazmida. U eksperimentima čišćenja od plazmida utvrđeno je da se geni za sintezu i imunost na bakteriocine nalaze na plazmidima. Pored toga, BGSM1-19 pokazuje antimikrobnu aktivnost na ispitivane patogene bakterije kao što su Salmonella paratyphi, Micrococcus flavus, Pseudomonas aeruginosa i Staphylococcus aureus., The strain Lactococcus lactis subsp. lactis BGSM1-19, isolated from traditionally homemade white cheese, produces two bacteriocins: lactococcin B-like bacteriocin named bacteriocin BacSMa and bacteriocin BacSMb which have shown similarity with lacticin RM. Plasmid curing resulted in a low yield (0.33%) of BacSMa- BacSMas and BacSMa- BacSMas, BacSMb-, BacSMbs derivatives. The bacteriocin biosynthesis was observed in the logarithmic phase of growth and the production plateau was reached after 8 h of incubation at 30oC, when the culture entered the early stationary phase. Biochemical characterization showed that strain BGSM1-19 retained antimicrobial activity within the pH range of 1 to 12 or after treatment at 100oC for 15 min. However, bacteriocin activity was completely lost after treatment with different proteolytic enzymes. The strain BGSM1-19 contains five plasmids. Plasmid curing indicated that genes coding for bacteriocins synthesis and immunity seem to be located on plasmids. BGSM1-19 exhibited antimicrobial activity against some pathogenic bacteria such as Salmonella paratyphi, Micrococcus flavus, Pseudomonas aeruginosa and Staphylococcus aureus.",
publisher = "Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd",
journal = "Acta Veterinaria-Beograd",
title = "Karakterizacija i antimikrobna aktivnost prirodnog izolata Lactococcus lactis subsp. lactis BGSM1-19, Characterization and antimicrobial activity of natural isolate Lactococcus lactis subsp. lactis BGSM1-19",
pages = "521-509",
number = "5-6",
volume = "57",
doi = "10.2298/AVB0706509S"
}

Strahinić, I., Cvetanović, D., Kojić, M., Fira, Đ., Tolinački, M.,& Topisirović, L.. (2007). Karakterizacija i antimikrobna aktivnost prirodnog izolata Lactococcus lactis subsp. lactis BGSM1-19. in Acta Veterinaria-Beograd
Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd., 57(5-6), 509-521.
https://doi.org/10.2298/AVB0706509S

Strahinić I, Cvetanović D, Kojić M, Fira Đ, Tolinački M, Topisirović L. Karakterizacija i antimikrobna aktivnost prirodnog izolata Lactococcus lactis subsp. lactis BGSM1-19. in Acta Veterinaria-Beograd. 2007;57(5-6):509-521.
doi:10.2298/AVB0706509S .

Strahinić, Ivana, Cvetanović, D., Kojić, Milan, Fira, Đorđe, Tolinački, Maja, Topisirović, Ljubiša, "Karakterizacija i antimikrobna aktivnost prirodnog izolata Lactococcus lactis subsp. lactis BGSM1-19" in Acta Veterinaria-Beograd, 57, no. 5-6 (2007):509-521,
https://doi.org/10.2298/AVB0706509S . .

TY  - JOUR
AU  - Topisirović, Ljubiša
AU  - Veljović, Katarina
AU  - Terzić-Vidojević, Amarela
AU  - Strahinić, Ivana
AU  - Kojić, Milan
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/816
AB  - Tradicionalni zlatarski sir pripada grupi belih, polutvrdih sireva proizvedenih u domaćinstvu. Sir se proizvodi od nepasterizovanog kravljeg mleka bez dodavanja bilo kakvih poznatih starter kultura. Ukupno je izolovano 253 Gram pozitivnih i katalaza negativnih bakterija mlečne kiseline (BMK). Rezultati su pokazali da 70 od 253 analiziranih izolata proizvodi antimikrobna jedinjenja poznatih kao bakteriocini. Većina izolata koji pripadaju rodovima Lactococcus i Enterococcus, kao i izolati vrsta Lactobacillus plantarum i Lb. brevis ne sintetišu ekstracelularne proteinaze. Nasuprot njima, izolati prodvrste Lb. paracasei subsp. paracasei pokazuju veoma dobru proteolitičku aktivnoist. Pokazano je da ne postoji korelacija između dobre proteolitičke i antimikrobne aktivnosti u većini izolata.
AB  - Traditional artisan Zlatar cheese belongs to the group of white, semi hard home-made cheeses, which are produced from no pasteurized cow's milk, without addition of any known bacterial starter culture. In total, 253 Gram-positive and catalase negative lactic acid bacteria (LAB) were isolated. Results showed that 70 out of 253 analyzed isolates produced antimicrobial compounds known as bacteriocins. Most isolates from genera Lactococcus and Enterococcus, and isolates belonging to species Lactobacillus plantarum and Lb. brevis, do not synthesize extracellular proteinase. In contrast, isolates from subspecies Lb. paracasei subsp. paracasei showed very good proteolytic activity. It was observed that good proteolytic activity of isolates was not in correlation with their good antimicrobial activity in the most of isolates.
PB  - Društvo genetičara Srbije, Beograd
T2  - Genetika-Belgrade
T1  - Komparativna analiza antimikrobne i proteolitičke aktivnosti bakterija mlečne kiseline izolovanih iz zlatarskog sira
T1  - Comparative analysis of antimicrobial and proteolytic activity of lactic acid bacteria isolated from Zlatar cheese
EP  - 138
IS  - 2
SP  - 125
VL  - 39
UR  - https://hdl.handle.net/21.15107/rcub_intor_816
ER  - 

@article{
author = "Topisirović, Ljubiša and Veljović, Katarina and Terzić-Vidojević, Amarela and Strahinić, Ivana and Kojić, Milan",
year = "2007",
abstract = "Tradicionalni zlatarski sir pripada grupi belih, polutvrdih sireva proizvedenih u domaćinstvu. Sir se proizvodi od nepasterizovanog kravljeg mleka bez dodavanja bilo kakvih poznatih starter kultura. Ukupno je izolovano 253 Gram pozitivnih i katalaza negativnih bakterija mlečne kiseline (BMK). Rezultati su pokazali da 70 od 253 analiziranih izolata proizvodi antimikrobna jedinjenja poznatih kao bakteriocini. Većina izolata koji pripadaju rodovima Lactococcus i Enterococcus, kao i izolati vrsta Lactobacillus plantarum i Lb. brevis ne sintetišu ekstracelularne proteinaze. Nasuprot njima, izolati prodvrste Lb. paracasei subsp. paracasei pokazuju veoma dobru proteolitičku aktivnoist. Pokazano je da ne postoji korelacija između dobre proteolitičke i antimikrobne aktivnosti u većini izolata., Traditional artisan Zlatar cheese belongs to the group of white, semi hard home-made cheeses, which are produced from no pasteurized cow's milk, without addition of any known bacterial starter culture. In total, 253 Gram-positive and catalase negative lactic acid bacteria (LAB) were isolated. Results showed that 70 out of 253 analyzed isolates produced antimicrobial compounds known as bacteriocins. Most isolates from genera Lactococcus and Enterococcus, and isolates belonging to species Lactobacillus plantarum and Lb. brevis, do not synthesize extracellular proteinase. In contrast, isolates from subspecies Lb. paracasei subsp. paracasei showed very good proteolytic activity. It was observed that good proteolytic activity of isolates was not in correlation with their good antimicrobial activity in the most of isolates.",
publisher = "Društvo genetičara Srbije, Beograd",
journal = "Genetika-Belgrade",
title = "Komparativna analiza antimikrobne i proteolitičke aktivnosti bakterija mlečne kiseline izolovanih iz zlatarskog sira, Comparative analysis of antimicrobial and proteolytic activity of lactic acid bacteria isolated from Zlatar cheese",
pages = "138-125",
number = "2",
volume = "39",
url = "https://hdl.handle.net/21.15107/rcub_intor_816"
}

Topisirović, L., Veljović, K., Terzić-Vidojević, A., Strahinić, I.,& Kojić, M.. (2007). Komparativna analiza antimikrobne i proteolitičke aktivnosti bakterija mlečne kiseline izolovanih iz zlatarskog sira. in Genetika-Belgrade
Društvo genetičara Srbije, Beograd., 39(2), 125-138.
https://hdl.handle.net/21.15107/rcub_intor_816

Topisirović L, Veljović K, Terzić-Vidojević A, Strahinić I, Kojić M. Komparativna analiza antimikrobne i proteolitičke aktivnosti bakterija mlečne kiseline izolovanih iz zlatarskog sira. in Genetika-Belgrade. 2007;39(2):125-138.
https://hdl.handle.net/21.15107/rcub_intor_816 .

Topisirović, Ljubiša, Veljović, Katarina, Terzić-Vidojević, Amarela, Strahinić, Ivana, Kojić, Milan, "Komparativna analiza antimikrobne i proteolitičke aktivnosti bakterija mlečne kiseline izolovanih iz zlatarskog sira" in Genetika-Belgrade, 39, no. 2 (2007):125-138,
https://hdl.handle.net/21.15107/rcub_intor_816 .