- PII
- S19982860S0132342325040071-1
- DOI
- 10.7868/S1998286025040071
- Publication type
- Article
- Status
- Published
- Authors
- Volume/ Edition
- Volume 51 / Issue number 4
- Pages
- 627-635
- Abstract
- Hemolysin II (HlyII) is one of the key pathogenic factors of the opportunistic gram-positive bacterium Bacillus cereus. HlyII lyses target cells by forming pores on membranes. HlyII belongs to the group of β-pore-forming toxins. A distinctive feature of HlyII is the presence of a C-terminal domain of 94 amino acid residues (HlyIICTD). It was shown that under slightly acidic conditions (pH 5.0), corresponding to the near-membrane region, the C-terminal domains, both by themselves and as part of the toxin, form stable complexes consisting of full-length and truncated toxin molecules. HlyII, HlyIILCTD (large C-terminal fragment Met225–Ile412) and HlyIICTD were obtained using recombinant producer strains Escherichia coli BL21(DE3). Biotinylation of HlyIICTD was carried out using N-hydroxysuccinimide ester of biotin. The interaction of HlyIICTD with HlyIICTD, HlyIILCTD, and HlyII, as well as the interaction of HlyIICTD with erythrocyte membranes, were studied by enzyme-linked immunosorbent assay and immunoblotting using both horseradish peroxidase-conjugated streptavidin and monoclonal antibodies against HlyII. Under slightly acidic conditions, HlyIICTD interacted with both the HlyIICTD domain within the full-length toxin and with the HlyIICTD protein. The interaction of HlyIICTD with the erythrocyte membrane increased fold in the presence of the toxin. The property of the C-terminal domain to form complexes with each other was revealed, regardless of whether it is part of the full-length toxin, the large C-terminal fragment, or the short HlyIICTD under conditions corresponding to those existing near the cell membrane (pH 5.0). The toxin in the peri membrane region exists in a partially molten globule state, in which the C-terminal domains of the monomers can bind to each other, increasing the local concentration of full-length toxins.
- Keywords
- порообразующий токсин C-концевой домен гемолизина II Bacillus cereus конформация белков плазматическая мембрана иммуноферментный анализ
- Date of publication
- 12.02.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 13
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