Literature DB >> 6895326

Effect of streptolysin S on liposomes. Influence of membrane lipid composition on toxin action.

J L Duncan, L Buckingham.   

Abstract

The effect of the bacterial cytolytic toxin, streptolysin S, on liposomes composed of various phospholipids was investigated. Large unilamellar vesicles containing [14C]sucrose were prepared by reverse-phase evaporation, and membrane damage produced by the toxin was measured by following the release of labeled marker. The net charge of the liposomes had little or no effect on their susceptibility to steptolysin S and the toxin was about equally effective on liposomes composed of phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine and phosphatidylglycerol. Experiments with liposomes composed of synthetic phospholipids showed that the ability of the toxin to produce membrane damage depended on the degree of unsaturation of the fatty acyl chains. The order of sensitivity was C18 : 2 phosphatidylcholine greater than C18: I phosphatidylcholine greater than C18 : 0 phosphatidylcholine = C16 : 0 phosphatidylcholine. Liposomes containing the latter two phospholipids were virtually unaffected by streptolysin S, and experiments with C18 : 0 phosphatidylcholine suggested that toxin activity does not bind to liposomes composed of phospholipids with saturated fatty acyl chains. The inclusion of 40 mol% cholesterol in C16 : 0 phosphatidylcholine and C18 : 0 phosphatidylcholine liposomes made these vesicles sensitive to streptolysin S. Egg phosphatidylcholine liposomes, which were unaffected at 0 degrees C and 4 degrees C became susceptible to the toxin at these temperatures when cholesterol was included. Liposomes composed of C14 : 0 phosphatidylcholine were unaffected by streptolysin S at temperatures below the chain-melting transition temperature (23 degrees C) of this phospholipid, but became increasingly susceptible above this temperature. The results suggest that the fluidity of the phospholipid hydrocarbon chains in the membrane is important in streptolysin S action.

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Year:  1981        PMID: 6895326     DOI: 10.1016/0005-2736(81)90119-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Cell membrane interaction of Bacillus thuringiensis subsp. israelensis cytolytic toxins.

Authors:  S S Gill; G J Singh; J M Hornung
Journal:  Infect Immun       Date:  1987-05       Impact factor: 3.441

2.  Non-covalent interaction of phospholipase A(2) (PLA(2)) and kaouthiotoxin (KTX) from venom of Naja kaouthia exhibits marked synergism to potentiate their cytotoxicity on target cells.

Authors:  Ashis K Mukherjee
Journal:  J Venom Res       Date:  2010-09-30
  2 in total

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