A5053194777- Bacillus and Francisella bacterial research
- Bacteriophages and microbial interactions
- Bacterial Genetics and Biotechnology
- Yersinia bacterium, plague, ectoparasites research
- Nanopore and Nanochannel Transport Studies
- Microbial infections and disease research
- Lipid Membrane Structure and Behavior
- Animal Genetics and Reproduction
- Plant-based Medicinal Research
- Plant Pathogenic Bacteria Studies
- Biopolymer Synthesis and Applications
- Insect Resistance and Genetics
- Clostridium difficile and Clostridium perfringens research
- Chromium effects and bioremediation
- Microbial Fuel Cells and Bioremediation
- Genomics and Phylogenetic Studies
- Metal Extraction and Bioleaching
- Botulinum Toxin and Related Neurological Disorders
- Vibrio bacteria research studies
- Monoclonal and Polyclonal Antibodies Research
- CRISPR and Genetic Engineering
- Bacterial Identification and Susceptibility Testing
- Viral Infections and Outbreaks Research
- RNA Interference and Gene Delivery
- Microbial Inactivation Methods
G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms
1999-2024
Russian Academy of Sciences
2015-2023
Institute of Bioorganic Chemistry
2023
Institute of Cell Biophysics
1991
Bacillus cereus is the fourth most common cause of foodborne illnesses that produces a variety pore-forming proteins as main pathogenic factors. B. hemolysin II (HlyII), belonging to β-barrel toxins, has C-terminal extension 94 amino acid residues designated HlyIICTD. An analysis panel monoclonal antibodies recombinant HlyIICTD protein revealed ability antibody HlyIIC-20 inhibit HlyII hemolysis. A conformational epitope recognized by was found. method peptide phage display and found it...
Bacillus cereus hemolysin II, a pore-forming β-barrel toxin (HlyII), has C-terminal extension of 94 amino acid residues, designated as the domain HlyII (HlyIICTD). HlyIICTD is capable forming oligomers in aqueous solutions. Oligomerization significantly increased presence erythrocytes and liposomes. Its affinity for various origins differed insignificantly but was noticeably higher T-cells. destroyed THP-1 monocytes J774 macrophages, acted most effectively on Jurkat T-lymphocytes had...
The almost complete sequence of the 16S rRNA gene Gram-positive polysporogenic bacterium Anaerobacter polyendosporus was determined. This allowed phylogenetic analysis A. by comparing sequences this to similar genes other bacteria. It shown that belongs Clostridium cluster I, subcluster Phylogenetically, is distantly related another polysporogenic, but non-cultivatable, bacterium, 'Metabacterium polyspora' and can be satisfactorily clustered within saccharolytic clostridia with a low DNA G+C...
Hemolysin II (HlyII) is one of the virulence factors opportunistic bacterium Bacillus cereus belonging to group β-pore-forming toxins. This work created a genetic construct encoding large C-terminal fragment toxin (HlyIILCTD, M225-I412 according numbering amino acid residues in HlyII). A soluble form HlyIILCTD was obtained using SlyD chaperone protein. first shown be capable agglutinating rabbit erythrocytes. Monoclonal antibodies against were by hybridoma technology. We also proposed mode...
Hemolysin II (HlyII)—one of the pathogenic factors Bacillus cereus, a pore-forming β-barrel toxin—possesses C-terminal extension 94 amino acid residues, designated as domain HlyII (HlyIICTD), which plays an important role in functioning toxin. Our previous work described monoclonal antibody (HlyIIC-20), capable strain-specific inhibition hemolysis caused by HlyII, and demonstrated dependence efficiency on presence proline at position 324 outside conformational antigenic determinant. In this...
The pathogenicity of many bacteria, including Bacillus cereus and Staphylococcus aureus, depends on pore-forming toxins (PFTs), which cause the lysis host cells by forming pores in membranes eukaryotic cells. Bioinformatic analysis revealed a region homologous to Lys171-Gly250 sequence hemolysin II (HlyII) from B. over 600 PFTs, we designated as "homologous peptide". Three β-barrel PFTs were used for detailed comparative analysis. Two them-HlyII cytotoxin K2 (CytK2)-are synthesized sensu...
Hemolysin II (HlyII) – one of the pathogenic factors Bacillus cereus, a pore-forming β-barrel toxin possesses C-terminal extension 94 amino acid residues, designated as domain HlyII (HlyIICTD), which plays an important role in functioning toxin. Our previous work described monoclonal antibody (HlyIIC-20), capable strain-specific inhibi-tion hemolysis caused by HlyII, and demonstrated dependence efficiency hemol-ysis on presence proline at position 324 outside conformational antigenic...
Pathogenicity of many bacteria including Bacillus cereus and Staphylococcus aureus depends on pore-forming toxins (PFTs), which cause lysis host cells by forming pores in membranes eukaryotic cells. Bioinformatic analysis revealed over 600 PFTs a region homologous to the Lys171-Gly250 sequence hemolysin II (HlyII) from B. cereus, we designated as “homologous peptide”. Three β-barrel were used for detailed comparative analysis. Two them –HlyII cytotoxin K2 (CytK2), – are synthesized sensu...