Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.

Abstract:

:Listeriolysin O (LLO) binds to cholesterol-containing membranes in which it oligomerizes to form pores. Preincubation of the toxin with cholesterol is known to inhibit haemolysis, whereas the oxidized form of cholesterol has no inhibitory effect. Using immunoblot analyses and flow cytometry we demonstrate that preincubation with cholesterol does not influence binding of the listeriolysin-cholesterol complex to red blood cells, eukaryotic cells or artificial membranes. Lytic activity of membrane-bound LLO inactivated by cholesterol can be restored by enzymatic treatment with cholesterol oxidase. To determine the step at which cholesterol inhibits lytic activity, we looked for pore formation using electron microscopy. Pores formed by purified listeriolysin could be directly visualized using erythrocyte ghosts. This property was lost upon incubation of the toxin with cholesterol. Quantitative analysis strongly suggest that inhibition of lysis by cholesterol is not due to decreased binding of listeriolysin to target membranes, but rather to an interference with a subsequent step leading to polymerization of the toxin.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Jacobs T,Darji A,Frahm N,Rohde M,Wehland J,Chakraborty T,Weiss S

doi

10.1046/j.1365-2958.1998.00858.x

subject

Has Abstract

pub_date

1998-06-01 00:00:00

pages

1081-9

issue

6

eissn

0950-382X

issn

1365-2958

journal_volume

28

pub_type

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