Description of a new potential aggregation factor from the Streptococcus thermophilus genome
Само за регистроване кориснике
2024
Аутори
Tsibulskaya, DaryaBlagojević, Veljko
Terzić-Vidojević, Amarela
Lukić, Ivana
Vasić, Marko
Dragačević, Luka
Kojić, Milan
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Autoaggregation, the ability to self-aggregate, is widespread among both Gram-positive and Gram-negative bacteria. The functional role of aggregation is not fully understood, but it is believed to be involved in the adaptation of bacteria to environmental conditions (PMID: 31294207). One interesting class of compounds responsible for the aggregation of lactic acid bacteria is aggregation factors—surface high-molecular-weight proteins rich in threonine and lysine (PMID: 30027759). Recently, our research group discovered a new strain of Streptococcus thermophilus in the mountainous regions of Serbia, exhibiting an aggregation phenotype. Aggregation phenotype was confirmed visually and using microscopy. Complete genome of Agg+ strain was sequenced using NGS and a gene encoding a potential aggregation factor, which was named aggS was identified. The predicted threonine (12.5%) and lysine (10.5%) rich protein contains 2367 amino acids, with an average molecular weight of 255986.63 Da. AggS ...also contains two cysteine residues, whereas previously well-described aggregation factors of this type did not contain any cysteine residues. The predicted protein includes an N-terminal YSIRK-like signal sequence and an LPXTG cell wall anchor domain. It has 6 Mucin binding domain repeats alternating with 6 Mub B2-like domain repeats. Additionally, we found a region resembling an ice-binding domain. Given that these bacteria endure prolonged periods of low temperatures, it can be speculated that this surface membrane protein also helps the bacteria withstand freezing. The fact that the alignment using BLASTp revealed AggS to be most closely related to an uncharacterised protein from the genome of Lactococcus garvieae, along with the discovery of a transposase gene sequence upstream of the gene, suggests that the aggregation factor was likely acquired through horizontal gene transfer. We plan to clone it into a shuttle vector and investigate the aggregation phenotype using a heterologous expression system in Lactococcus lactis, as well as explore its other functions.
Кључне речи:
aggregation / NGS analysis / LactobacillalesИзвор:
XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april, 2024, 110-110Издавач:
- Serbian Society for Microbiology
Институција/група
TorlakTY - CONF AU - Tsibulskaya, Darya AU - Blagojević, Veljko AU - Terzić-Vidojević, Amarela AU - Lukić, Ivana AU - Vasić, Marko AU - Dragačević, Luka AU - Kojić, Milan PY - 2024 UR - http://intor.torlakinstitut.com/handle/123456789/875 AB - Autoaggregation, the ability to self-aggregate, is widespread among both Gram-positive and Gram-negative bacteria. The functional role of aggregation is not fully understood, but it is believed to be involved in the adaptation of bacteria to environmental conditions (PMID: 31294207). One interesting class of compounds responsible for the aggregation of lactic acid bacteria is aggregation factors—surface high-molecular-weight proteins rich in threonine and lysine (PMID: 30027759). Recently, our research group discovered a new strain of Streptococcus thermophilus in the mountainous regions of Serbia, exhibiting an aggregation phenotype. Aggregation phenotype was confirmed visually and using microscopy. Complete genome of Agg+ strain was sequenced using NGS and a gene encoding a potential aggregation factor, which was named aggS was identified. The predicted threonine (12.5%) and lysine (10.5%) rich protein contains 2367 amino acids, with an average molecular weight of 255986.63 Da. AggS also contains two cysteine residues, whereas previously well-described aggregation factors of this type did not contain any cysteine residues. The predicted protein includes an N-terminal YSIRK-like signal sequence and an LPXTG cell wall anchor domain. It has 6 Mucin binding domain repeats alternating with 6 Mub B2-like domain repeats. Additionally, we found a region resembling an ice-binding domain. Given that these bacteria endure prolonged periods of low temperatures, it can be speculated that this surface membrane protein also helps the bacteria withstand freezing. The fact that the alignment using BLASTp revealed AggS to be most closely related to an uncharacterised protein from the genome of Lactococcus garvieae, along with the discovery of a transposase gene sequence upstream of the gene, suggests that the aggregation factor was likely acquired through horizontal gene transfer. We plan to clone it into a shuttle vector and investigate the aggregation phenotype using a heterologous expression system in Lactococcus lactis, as well as explore its other functions. PB - Serbian Society for Microbiology C3 - XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april T1 - Description of a new potential aggregation factor from the Streptococcus thermophilus genome EP - 110 SP - 110 UR - https://hdl.handle.net/21.15107/rcub_intor_875 ER -
@conference{ author = "Tsibulskaya, Darya and Blagojević, Veljko and Terzić-Vidojević, Amarela and Lukić, Ivana and Vasić, Marko and Dragačević, Luka and Kojić, Milan", year = "2024", abstract = "Autoaggregation, the ability to self-aggregate, is widespread among both Gram-positive and Gram-negative bacteria. The functional role of aggregation is not fully understood, but it is believed to be involved in the adaptation of bacteria to environmental conditions (PMID: 31294207). One interesting class of compounds responsible for the aggregation of lactic acid bacteria is aggregation factors—surface high-molecular-weight proteins rich in threonine and lysine (PMID: 30027759). Recently, our research group discovered a new strain of Streptococcus thermophilus in the mountainous regions of Serbia, exhibiting an aggregation phenotype. Aggregation phenotype was confirmed visually and using microscopy. Complete genome of Agg+ strain was sequenced using NGS and a gene encoding a potential aggregation factor, which was named aggS was identified. The predicted threonine (12.5%) and lysine (10.5%) rich protein contains 2367 amino acids, with an average molecular weight of 255986.63 Da. AggS also contains two cysteine residues, whereas previously well-described aggregation factors of this type did not contain any cysteine residues. The predicted protein includes an N-terminal YSIRK-like signal sequence and an LPXTG cell wall anchor domain. It has 6 Mucin binding domain repeats alternating with 6 Mub B2-like domain repeats. Additionally, we found a region resembling an ice-binding domain. Given that these bacteria endure prolonged periods of low temperatures, it can be speculated that this surface membrane protein also helps the bacteria withstand freezing. The fact that the alignment using BLASTp revealed AggS to be most closely related to an uncharacterised protein from the genome of Lactococcus garvieae, along with the discovery of a transposase gene sequence upstream of the gene, suggests that the aggregation factor was likely acquired through horizontal gene transfer. We plan to clone it into a shuttle vector and investigate the aggregation phenotype using a heterologous expression system in Lactococcus lactis, as well as explore its other functions.", publisher = "Serbian Society for Microbiology", journal = "XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april", title = "Description of a new potential aggregation factor from the Streptococcus thermophilus genome", pages = "110-110", url = "https://hdl.handle.net/21.15107/rcub_intor_875" }
Tsibulskaya, D., Blagojević, V., Terzić-Vidojević, A., Lukić, I., Vasić, M., Dragačević, L.,& Kojić, M.. (2024). Description of a new potential aggregation factor from the Streptococcus thermophilus genome. in XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april Serbian Society for Microbiology., 110-110. https://hdl.handle.net/21.15107/rcub_intor_875
Tsibulskaya D, Blagojević V, Terzić-Vidojević A, Lukić I, Vasić M, Dragačević L, Kojić M. Description of a new potential aggregation factor from the Streptococcus thermophilus genome. in XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april. 2024;:110-110. https://hdl.handle.net/21.15107/rcub_intor_875 .
Tsibulskaya, Darya, Blagojević, Veljko, Terzić-Vidojević, Amarela, Lukić, Ivana, Vasić, Marko, Dragačević, Luka, Kojić, Milan, "Description of a new potential aggregation factor from the Streptococcus thermophilus genome" in XIII Congress of microbiologists of Serbia with international participation, Mikromed regio 5, From biotechnology to human and planetary health, 4-6 april (2024):110-110, https://hdl.handle.net/21.15107/rcub_intor_875 .