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首页> 外文期刊>The FEBS journal >Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin
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Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin

机译：霍乱弧菌溶血素的单点突变破坏了毒素的膜孔形成机制

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摘要

Vibrio cholerae cytolysin (VCC) belongs to the family of b-barrel poreforming protein toxins. VCC is secreted by the bacteria as water-soluble monomers, which upon binding to target eukaryotic cells form transmembrane heptameric b-barrel channels. High-resolution 3D structures are described both for the water-soluble monomeric form and the transmembrane oligomeric pore; albeit that our understanding of the mechanistic details of the membrane pore-formation process remains incomplete. Here, we report the characterization of a nonfunctional VCC variant harboring a single point mutation of Ala425Val positioned within a potential membrane-interacting loop in the VCC structure. The mutation appears to affect interaction of the toxin with erythrocytes as well as cholesterolcontaining liposome membrane, without affecting the oligomerization ability of the membrane-bound toxin molecules. The membrane-bound oligomers formed by this VCC mutant do not appear to represent the functional pore assembly of the toxin; rather, such assembly could be considered as being trapped in an abortive, nonfunctional oligomeric state. Our results suggest that the Ala425Val mutation in VCC critically compromises its cholesterol-dependent membrane-interaction mechanism and also abrogates the process of functional membrane pore formation by the toxin.
机译：霍乱弧菌溶血素（VCC）属于b-桶造孔蛋白毒素家族。 VCC由细菌分泌为水溶性单体，其与靶真核细胞结合后形成跨膜七聚体b-桶通道。针对水溶性单体形式和跨膜低聚孔均描述了高分辨率的3D结构。尽管我们对膜孔形成过程的机械细节的理解仍然不完整。在这里，我们报告的非功能性VCC变体的特征在于它具有Ala425Val的单点突变，该变体位于VCC结构中潜在的膜相互作用环内。该突变似乎影响毒素与红细胞以及含胆固醇的脂质体膜的相互作用，而不影响膜结合毒素分子的寡聚能力。该VCC突变体形成的与膜结合的寡聚体似乎并不代表该毒素的功能性孔组装。相反，可以认为这种组装被困在堕胎的，无功能的寡聚状态。我们的结果表明，VCC中的Ala425Val突变严重损害了其胆固醇依赖性膜相互作用机制，并且也消除了毒素导致的功能性膜孔形成过程。

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