Linked Life Data

10623563

Source:http://linkedlifedata.com/resource/pubmed/id/10623563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-2-7
pubmed:abstractText
Beta-toxin is one of the lethal toxins of Clostridium perfringens. It shares sequence homology with the pore-forming alpha-toxin of Staphylococcus aureus and structural homology has been indicated by mutagenesis studies. Human endothelial cells are sensitive to the toxic effect of alpha-toxin and in order to investigate the function of beta-toxin we have looked at the effect of the protein on human umbilical vein endothelial cells. We show that like alpha-toxin beta-toxin induces release of arachidonic acid in a dose dependent manner. In addition we show that both toxins cause leakage of inositol from the cells, consistent with the formation of transmembrane pores. The effect of toxin mutants on endothelial cells correlates with the lethal dose of each mutant in mice. Furthermore, we demonstrate the formation of heat stable toxin multimers in the cell membrane. Multimer formation was not observed on other cell types tested. We conclude that beta-toxin is a cell specific pore-forming toxin, structurally and functionally related to alpha-toxin of Staphylococcus aureus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0882-4010
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-50
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells.
pubmed:affiliation
Institute for Experimental Pathology, University of Iceland, Reykjavik, Keldur, 112, Iceland. vstein@decode.is
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't