Linked Life Data

2004111

Source:http://linkedlifedata.com/resource/pubmed/id/2004111

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-4-25
pubmed:abstractText
We have studied the kinetics of staphylococcal alpha-toxin oligomerisation in relation to membrane permeabilisation, using as targets cultured adrenocortical Y1 cells, rabbit red blood cells (RRBC), human platelets, and liposomes prepared of lipids extracted from platelets. After isolation of membranes from toxin-treated cells, oligomeric toxin was detected (i) by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE) followed by autoradiography or Western blotting, and (ii) by electron microscopy of negatively stained specimens. alpha-Toxin was found to oligomerise on all membranes independently of the temperature. On RRBC and Y1 cells most of the membrane associated toxin appeared converted to the oligomeric form. Hexamers were always present along with membrane permeabilisation. However, hexamers were also detected at conditions when membrane permeabilisation did not occur; at low temperature, in the presence of high concentrations of Ca2+, and after pretreatment of cells with concanavalin A (Con A). Addition of a neutralising monoclonal antibody (MAb) to cell-bound toxin collected it into aggregates much larger than the hexamers. By contrast hexameric toxin remained after addition of a non-neutralising MAb. Our data suggest that the active toxin species is not monomeric, and support the hypothesis that alpha-toxin permeabilises membranes by forming hexameric protein-lined transmembrane channels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
1062
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Oligomerisation of cell-bound staphylococcal alpha-toxin in relation to membrane permeabilisation.
pubmed:affiliation
Department of Bacteriology, Karolinska Institutet, Stockholm, Sweden.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't