A High-Homology Region Provides the Possibility of Detecting β-Barrel Pore-Forming Toxins from Various Bacterial Species.

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.

Genomic analysis and assessment of pathogenic (toxicogenic) potential of Staphylococcus haemolyticus and Bacillus paranthracis consortia isolated from bovine mastitis in Russia.

Three stable microbial consortia, each composed of Bacillus paranthracis and Staphylococcus haemolyticus strains, were isolated from milk of cows diagnosed with mastitis in three geographically remote regions of Russia. The composition of these consortia remained stable following multiple passages on culture media. Apparently, this stability is due to the structure of the microbial biofilms formed by the communities.

The Effects of Zirconium and Yttrium Addition on the Microstructure and Hardness of AlCuMgMn Alloy when Applying In Situ Heating during the Laser Melting Process.

This paper studies the effect of the laser melting process (LMP) on the microstructure and hardness of a new modified AlCuMgMn alloy with zirconium (Zr) and Yttrium (Y) elements. Homogenized (480 °C/8 h) alloys were laser-surface-treated at room temperature and a heating platform with in situ heating conditions was used in order to control the formed microstructure by decreasing the solidification rate in the laser-melted zone (LMZ). Modifying the AlCuMgMn alloy with 0.

Region Met225 to Ile412 of Hemolysin II Is Capable to Agglutinate Red Blood Cells.

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.