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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 |
1991-10-2
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pubmed:abstractText |
A 10-amino-acid repeating sequence of the hemagglutinating portion of Clostridium difficile toxin A has been synthesized and used to produce antisera in rabbits. Antipeptide antibody inhibited toxin A-mediated hemagglutination and neutralized cytotoxic activity. Immunoblot analysis with the antipeptide antibody revealed cross-reactivity with native toxin, a recombinant protein containing the toxin A repeats, and a glucan-binding protein from Streptococcus mutans whose primary structure has repeating amino acid motifs similar to those of the synthetic peptide. A polyclonal antibody against the glucan-binding protein, which cross-reacted with purified toxin A, also inhibited toxin A-mediated hemagglutination and neutralized cytotoxic activity. We recently identified toxin A and the glucan-binding protein as members of a novel family of clostridial and streptococcal binding proteins based on conserved repeating amino acid motifs at the C-terminal region of the molecules. This study provides immunological and functional evidence of the predicted relationship between toxin A and the glucan-binding protein and further implicates the repeating subunits as ligand-binding domains in this family of proteins.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-1670930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-1830357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2105276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2112562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2118549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2118866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2148295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2150909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2307516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2428826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2463969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-2961615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-3040686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-3123524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-3144429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-3527044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-3917975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-7399686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1715320-927200
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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/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucans,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glucan-binding proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tcdA protein, Clostridium difficile
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0019-9567
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3151-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1715320-Amino Acid Sequence,
pubmed-meshheading:1715320-Animals,
pubmed-meshheading:1715320-Antibodies, Bacterial,
pubmed-meshheading:1715320-Bacterial Toxins,
pubmed-meshheading:1715320-Carrier Proteins,
pubmed-meshheading:1715320-Clostridium difficile,
pubmed-meshheading:1715320-Cross Reactions,
pubmed-meshheading:1715320-Cytotoxicity, Immunologic,
pubmed-meshheading:1715320-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1715320-Enterotoxins,
pubmed-meshheading:1715320-Epitopes,
pubmed-meshheading:1715320-Glucans,
pubmed-meshheading:1715320-Hemagglutination,
pubmed-meshheading:1715320-Immunoblotting,
pubmed-meshheading:1715320-Lectins,
pubmed-meshheading:1715320-Molecular Sequence Data,
pubmed-meshheading:1715320-Oligopeptides,
pubmed-meshheading:1715320-Rabbits,
pubmed-meshheading:1715320-Recombinant Proteins,
pubmed-meshheading:1715320-Streptococcus mutans,
pubmed-meshheading:1715320-Tumor Cells, Cultured
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pubmed:year |
1991
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pubmed:articleTitle |
Antigenic cross-reactivity and functional inhibition by antibodies to Clostridium difficile toxin A, Streptococcus mutans glucan-binding protein, and a synthetic peptide.
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pubmed:affiliation |
Department of Medical Microbiology, St. Bartholomew's Hospital Medical College, West Smithfield, London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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