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• W2011606192 abstract "Listeriolysin O (LLO) is a cholesterol-dependent cytolysin that is an essential virulence factor of Listeria monocytogenes . LLO pore-forming activity is pH-dependent; it is active at acidic pH (<6), but not at neutral pH. In contrast to other pH-dependent toxins, we have determined that LLO pore-forming activity is controlled by a rapid and irreversible denaturation of its structure at neutral pH at temperatures >30°C. Rapid denaturation is triggered at neutral pH by the premature unfolding of the domain 3 transmembrane β-hairpins; structures that normally form the transmembrane β-barrel. A triad of acidic residues within domain 3 function as the pH sensor and initiate the denaturation of LLO by destabilizing the structure of domain 3. These studies provide a view of a molecular mechanism by which the activity of a bacterial toxin is regulated by pH." @default.
• W2011606192 created "2016-06-24" @default.
• W2011606192 creator A5003305733 @default.
• W2011606192 creator A5044088516 @default.
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• W2011606192 date "2005-08-16" @default.
• W2011606192 modified "2023-09-30" @default.
• W2011606192 title "Molecular basis of listeriolysin O pH dependence" @default.
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• W2011606192 doi "https://doi.org/10.1073/pnas.0500558102" @default.
• W2011606192 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1194900" @default.
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