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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1989-11-17
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pubmed:abstractText |
Shiga toxin is a protein toxin produced by Shigella dysenteriae type I strains. In this report we present a procedure for the separation of functionally intact toxin A and B chains and for their reconstitution to form biologically active molecules. In agreement with the findings of others, the isolated A chain was shown to be a potent in vitro inhibitor of eukaryotic protein synthesis. The isolated B chain bound to HeLa cells and competitively inhibited the binding and cytotoxic activity of holotoxin. These findings show that the functional role of the B chain is to recognize cell surface functional receptors. By labelling the B subunit alone, prior to renaturation of holotoxin, the polypeptide chains were shown to associate noncovalently with a stoichiometry of one A chain and five B chains.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1231-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2677606-Bacterial Toxins,
pubmed-meshheading:2677606-Binding, Competitive,
pubmed-meshheading:2677606-Cross-Linking Reagents,
pubmed-meshheading:2677606-Cytotoxins,
pubmed-meshheading:2677606-HeLa Cells,
pubmed-meshheading:2677606-Humans,
pubmed-meshheading:2677606-Imidoesters,
pubmed-meshheading:2677606-Peptide Fragments,
pubmed-meshheading:2677606-Protein Biosynthesis,
pubmed-meshheading:2677606-Protein Conformation,
pubmed-meshheading:2677606-Shiga Toxins,
pubmed-meshheading:2677606-Shigella dysenteriae
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pubmed:year |
1989
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pubmed:articleTitle |
Isolation and characterization of functional Shiga toxin subunits and renatured holotoxin.
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pubmed:affiliation |
Department of Medicine, New England Medical Center, Boston, Massachusetts.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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