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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
27
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pubmed:dateCreated |
1993-10-20
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pubmed:abstractText |
The Yersinia pseudotuberculosis invasin protein is a 986-amino acid protein that promotes bacterial penetration into mammalian cells by avidly binding multiple beta 1-chain integrins. A 192-amino acid carboxyl-terminal domain of invasin was previously shown to be sufficient for binding. Evidence is presented here that a 76-amino acid disulfide loop in the integrin binding domain of invasin is required for invasin-mediated cell binding and entry. Bacterial mutants that were altered at either of 2 cysteine residues in the binding domain of invasin were completely defective for entry. Purified invasin protein derivatives altered at either of these cysteines, in contrast to the wild-type invasin, did not promote either cell binding or penetration. Analysis of proteolytic products of invasin in the presence or absence of reducing agent provided evidence of an intra-chain disulfide bond near the carboxyl terminus of the protein. Alkylation of invasin derivatives with [3H]iodoacetate indicated that these 2 cysteines were normally disulfide-bonded. A treatment that resulted in the maximal reduction of the disulfide bond also resulted in maximal loss of cell attachment activity. These results indicate that the 76-amino acid disulfide loop at the carboxyl terminus of invasin is required for recognition by integrins.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetates,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/invasin, Yersinia
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
268
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pubmed:geneSymbol |
inv
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20524-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8376409-Adhesins, Bacterial,
pubmed-meshheading:8376409-Amino Acid Sequence,
pubmed-meshheading:8376409-Bacterial Proteins,
pubmed-meshheading:8376409-Binding Sites,
pubmed-meshheading:8376409-Cloning, Molecular,
pubmed-meshheading:8376409-Codon,
pubmed-meshheading:8376409-Disulfides,
pubmed-meshheading:8376409-Dithiothreitol,
pubmed-meshheading:8376409-Escherichia coli,
pubmed-meshheading:8376409-Genes, Bacterial,
pubmed-meshheading:8376409-Humans,
pubmed-meshheading:8376409-Integrins,
pubmed-meshheading:8376409-Iodoacetates,
pubmed-meshheading:8376409-Iodoacetic Acid,
pubmed-meshheading:8376409-Kinetics,
pubmed-meshheading:8376409-Mutagenesis, Site-Directed,
pubmed-meshheading:8376409-Plasmids,
pubmed-meshheading:8376409-Point Mutation,
pubmed-meshheading:8376409-Recombinant Proteins,
pubmed-meshheading:8376409-Restriction Mapping,
pubmed-meshheading:8376409-Tumor Cells, Cultured,
pubmed-meshheading:8376409-Yersinia pseudotuberculosis
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pubmed:year |
1993
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pubmed:articleTitle |
A 76-amino acid disulfide loop in the Yersinia pseudotuberculosis invasin protein is required for integrin receptor recognition.
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pubmed:affiliation |
Department of Medicine, Tufts-New England Medical Center Hospital, Boston, Massachusetts 02111.
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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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