Publications by authors named "Alexander V Siunov"
The pathogenicity of many bacteria, including and , depends on pore-forming toxins (PFTs), which cause the lysis of host cells by forming pores in the membranes of eukaryotic cells. Bioinformatic analysis revealed a region homologous to the Lys171-Gly250 sequence in hemolysin II (HlyII) from in over 600 PFTs, which we designated as a "homologous peptide". Three β-barrel PFTs were used for a detailed comparative analysis.
View Article and Find Full Text PDFArticle Synopsis
- Researchers created 16 mutant versions of HlyIICTD to study how changes in its surface amino acids affect its interaction with a monoclonal antibody (HlyIIC-20), which inhibits hemolysis.
- The study found that certain mutations altered the structure of the antibody’s target site, confirming that flexibility in HlyIICTD is crucial for the toxin’s effectiveness, and identified specific amino acids (N339 and K340) that are important for the antibody binding.
Hemolysin II (HlyII) is one of the virulence factors of the opportunistic bacterium belonging to the group of β-pore-forming toxins. This work created a genetic construct encoding a large C-terminal fragment of the toxin (HlyIILCTD, M225-I412 according to the numbering of amino acid residues in HlyII). A soluble form of HlyIILCTD was obtained using the SlyD chaperone protein.
View Article and Find Full Text PDF