Anđelković, Uroš

Link to this page

Authority KeyName Variants
orcid::0000-0002-9992-9316
  • Anđelković, Uroš (4)
Projects

Author's Bibliography

Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart

Grozdanović, Milica; Ostojić, Sanja; Aleksić, Ivana; Anđelković, Uroš; Petersen, Arnd; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2014)

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Ostojić, Sanja
AU  - Aleksić, Ivana
AU  - Anđelković, Uroš
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/411
AB  - BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
EP  - 3052
IS  - 14
SP  - 3046
VL  - 94
DO  - 10.1002/jsfa.6656
UR  - conv_342
ER  - 
@article{
author = "Grozdanović, Milica and Ostojić, Sanja and Aleksić, Ivana and Anđelković, Uroš and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart",
pages = "3052-3046",
number = "14",
volume = "94",
doi = "10.1002/jsfa.6656",
url = "conv_342"
}
Grozdanović, M., Ostojić, S., Aleksić, I., Anđelković, U., Petersen, A.,& Gavrović-Jankulović, M.. (2014). Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 94(14), 3046-3052.
https://doi.org/10.1002/jsfa.6656
conv_342
Grozdanović M, Ostojić S, Aleksić I, Anđelković U, Petersen A, Gavrović-Jankulović M. Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture. 2014;94(14):3046-3052.
doi:10.1002/jsfa.6656
conv_342 .
Grozdanović, Milica, Ostojić, Sanja, Aleksić, Ivana, Anđelković, Uroš, Petersen, Arnd, Gavrović-Jankulović, Marija, "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart" in Journal of the Science of Food and Agriculture, 94, no. 14 (2014):3046-3052,
https://doi.org/10.1002/jsfa.6656 .,
conv_342 .
7
16
11
17

Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Burazer, Lidija; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Elsevier Ltd, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/388
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.
PB  - Elsevier Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
EP  - 59
SP  - 53
VL  - 94
DO  - 10.1016/j.phytochem.2013.06.006
UR  - conv_519
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.",
publisher = "Elsevier Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
pages = "59-53",
volume = "94",
doi = "10.1016/j.phytochem.2013.06.006",
url = "conv_519"
}
Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Elsevier Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006
conv_519
Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006
conv_519 .
Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 .,
conv_519 .
1
16
16
17

In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Grozdanović, Milica; Aleksić, Ivana; Gavrović-Jankulović, Marija

(Springer, New York, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/390
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
EP  - 105
IS  - 1
SP  - 100
VL  - 53
DO  - 10.1007/s12088-012-0319-2
UR  - conv_302
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
pages = "105-100",
number = "1",
volume = "53",
doi = "10.1007/s12088-012-0319-2",
url = "conv_302"
}
Popović, M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M.. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2
conv_302
Popović M, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology. 2013;53(1):100-105.
doi:10.1007/s12088-012-0319-2
conv_302 .
Popović, Milica, Anđelković, Uroš, Grozdanović, Milica, Aleksić, Ivana, Gavrović-Jankulović, Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" in Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 .,
conv_302 .
13
13
14

Molecular and immunological characterization of Mus a 5 allergen from banana fruit

Aleksić, Ivana; Popović, Milica; Dimitrijević, Rajna; Anđelković, Uroš; Vassilopoulou, Emilia; Sinaniotis, Athanassios; Atanasković-Marković, Marina; Lindner, Buko; Petersen, Arnd; Papadopoulos, Nikolaos G.; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2012)

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/362
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
EP  - 453
IS  - 3
SP  - 446
VL  - 56
DO  - 10.1002/mnfr.201100541
UR  - conv_286
ER  - 
@article{
author = "Aleksić, Ivana and Popović, Milica and Dimitrijević, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
pages = "453-446",
number = "3",
volume = "56",
doi = "10.1002/mnfr.201100541",
url = "conv_286"
}
Aleksić, I., Popović, M., Dimitrijević, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research
Wiley, Hoboken., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541
conv_286
Aleksić I, Popović M, Dimitrijević R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541
conv_286 .
Aleksić, Ivana, Popović, Milica, Dimitrijević, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition and Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 .,
conv_286 .
18
19
21