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Volume 153, Issue 7

Irreversible loss of membrane-binding activity of -derived cytolysins in non-acidic conditions: a distinct difference from allied cytolysins produced by other Gram-positive bacteria Free

Abstract

Listeriolysin O (LLO), a member of the cholesterol-dependent cytolysin (CDC) family, is a major virulence factor of and contributes to bacterial escape from intracellular killing of macrophages. LLO is activated under weakly acidic conditions; however, the molecular mechanism of this pH-dependent expression of cytolytic activity of LLO is poorly understood. In this study, CDCs including LLO, ivanolysin O (ILO), seeligeriolysin O (LSO), pneumolysin (PLY), streptolysin O (SLO) and perfringolysin O (PFO) were prepared as recombinant proteins and examined for their functional changes after treatment under various pH conditions. Haemolytic and membrane cholesterol-binding activities were not affected in PLY, SLO and PFO at any pH examined. By contrast, all the -derived cytolysins, LLO, ILO and LSO, were active only at an acidic pH and rapidly inactivated under neutral or alkaline conditions. Once inactivated, LLO could not be reactivated even by a downward pH shift. The hydrophobicity of LLO treated at neutral or alkaline pH was increased. These data suggested that the pH-dependent loss of cytolytic activity appeared to be due to irreversible structural changes of domain 4 that resulted in the loss of target membrane cholesterol binding.

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  • Accepted:
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Keyword(s): CDC, cholesterol-dependent cytolysin , HU, haemolytic unit , ILO, ivanolysin O , LDH, lactate dehydrogenase , LLO, listeriolysin , LSO, seeligeriolysin O , PFO, perfringolysin O , PLY, pneumolysin , SLO, streptolysin O , SRBC, sheep red blood cell and TNS, 2-(p-toluidinyl)naphthalene-6-sulfonic acid, sodium salt
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2007-07-01
2024-04-20
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Irreversible loss of membrane-binding activity of Listeria-derived cytolysins in non-acidic conditions: a distinct difference from allied cytolysins produced by other Gram-positive bacteria
Microbiology 153, 2250 (2007); https://doi.org/10.1099/mic.0.2007/005843-0
/content/journal/micro/10.1099/mic.0.2007/005843-0
/content/journal/micro/10.1099/mic.0.2007/005843-0
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