A method for the quantitation of homologous endopeptidases AlpA and AlpB from Lysobacter sp. XL1

Karatovskaya, Anna; Rudenko, N. V.; Tsfasman, I. M.; Guseva, Ksenya A.; Ламан, А. Г.; Boziev, Khanafi Magometovich; Бровко, Ф. А.; Vasilyeva, Natalia V.

doi:10.1016/j.procbio.2016.06.009

Cited by 7 publications

(4 citation statements)

References 18 publications

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“…Three days before cell fusion, 50 μg of conjugate in PBS was injected subcutaneously into each animal’s paws and intraperitoneally. Hybridomas secreting MAbs were obtained by hybridoma technology ( 8 ) with modifications ( 20 ).…”

Section: Methodsmentioning

confidence: 99%

Protective Capacity of Monoclonal Antibodies against Acinetobacter baumannii K9 Capsular Polysaccharide

et al. 2023

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Section: Methodsmentioning

confidence: 99%

Protective Capacity of Monoclonal Antibodies against Acinetobacter baumannii K9 Capsular Polysaccharide

et al. 2023

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“…Conjugation of the synthetic peptide DSFNTFYGNQLFMK (IQChem, Russia) with KLH was carried out as described [24]. Immunization of experimental animals was performed with a dose of 10 μg of peptide per 100 μg of KLH in Freund's adjuvant according to the scheme used for immunization with homologous peptide.…”

Section: Preparation and Purification Of Mabsmentioning

confidence: 99%

“…Immunization of experimental animals was performed with a dose of 10 μg of peptide per 100 μg of KLH in Freund's adjuvant according to the scheme used for immunization with homologous peptide. mAb-Secreting hybridomas were obtained using hybridoma technology [17] with modifications from [24]. Selection of hybridomas secreting specific antibodies was carried out by indirect ELISA by interaction of supracellular supernatants with HlyII and Hla immobilized on immunoplates.…”

Section: Preparation and Purification Of Mabsmentioning

confidence: 99%

A High-Homology Region in Bacterial β-Barrel Pore-Forming Toxins

Nagel,

Vetrova,

Rudenko

et al. 2024

Preprint

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Pathogenicity of many bacteria including Bacillus cereus and Staphylococcus aureus depends on pore-forming toxins (PFTs), which cause lysis of host cells by forming pores in membranes of eukaryotic cells. Bioinformatic analysis revealed in over 600 PFTs a region homologous to the Lys171-Gly250 sequence in hemolysin II (HlyII) from B. cereus, which we designated as “homologous peptide”. Three β-barrel PFTs were used for a detailed comparative analysis. Two of them –HlyII and cytotoxin K2 (CytK2), – are synthesized in Bacillus cereus sensu lato; the third – S. aureus α-toxin (Hla) – is the most investigated representative of the family. Protein modeling showed certain amino acids of homologous peptide to be located on the surface of the monomeric forms of these β-barrel PFTs. We obtained monoclonal antibodies against both a cloned homologous peptide and a 14-membered synthetic peptide DSFNTFYGNQLFMK as part of homologous peptide. The HlyII, CytK2 and Hla regions recognized by the obtained antibodies, as well as an antibody capable of suppressing the hemolytic activity of CytK2, were identified in the course of the work. Antibodies capable of recognizing PFTs of various origins can be useful tools for both identification and suppression of the cytolytic activity of PFTs.

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“…Three days before cell fusion, 10 µg HlyIILCTD in PBS was injected subcutaneously into each animal's paws and intraperitoneally. Hybridomas secreting MAbs were obtained by hybridoma technology [16] with modifications [24].…”

Section: Production and Isolation Of Mabsmentioning

confidence: 99%

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

et al. 2023

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Hemolysin II (HlyII) is one of the virulence factors of the opportunistic bacterium Bacillus cereus 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. HlyIILCTD was first shown to be capable of agglutinating rabbit erythrocytes. Monoclonal antibodies against HlyIILCTD were obtained by hybridoma technology. We also proposed a mode of rabbit erythrocyte agglutination by HlyIILCTD and selected three anti-HlyIILCTD monoclonal antibodies that inhibited the agglutination.

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A method for the quantitation of homologous endopeptidases AlpA and AlpB from Lysobacter sp. XL1

Cited by 7 publications

References 18 publications

Protective Capacity of Monoclonal Antibodies against Acinetobacter baumannii K9 Capsular Polysaccharide

Protective Capacity of Monoclonal Antibodies against Acinetobacter baumannii K9 Capsular Polysaccharide

A High-Homology Region in Bacterial β-Barrel Pore-Forming Toxins

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

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