| Heparin-inhibitable lectin activity of the filamentous hemagglutinin adhesin of Bordetella pertussis. | |
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MedLine Citation:
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PMID: 8112848 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Bordetella pertussis, the etiologic agent of whooping cough, produces an outer membrane-associated filamentous hemagglutinin (FHA) which is the major adhesin of this organism. FHA exhibits a lectin-like activity for heparin and dextran sulfate. By using in vitro adherence assays to cultured epithelial cells, the attachment of B. pertussis was reduced in the presence of sulfated polysaccharides such as heparin and dextran sulfate but not in the presence of dextran, indicating the crucial role of polysaccharide sulfation. In addition, inhibition of cellular sulfation by chlorate treatment of the cells resulted in a reduction of B. pertussis adherence, suggesting that epithelial cell surface-exposed sulfated glycoconjugates may serve as receptors for the microorganism. B. pertussis mutant strains deficient in FHA production expressed residual adherence that was no longer inhibited by sulfated polysaccharides. In addition, purified FHA displayed heparin-inhibitable binding to epithelial cells. Mapping experiments of the heparin-binding site of FHA indicated that this site is different from the RGD site and the recently proposed carbohydrate-binding site involved in the interaction of FHA with lactosylceramide. This result demonstrates that FHA contains at least three different binding sites, a feature unusual for bacterial adhesions but similar to features of eukaryotic adhesins and extracellular matrix proteins. |
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Authors:
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F D Menozzi; R Mutombo; G Renauld; C Gantiez; J H Hannah; E Leininger; M J Brennan; C Locht |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Infection and immunity Volume: 62 ISSN: 0019-9567 ISO Abbreviation: Infect. Immun. Publication Date: 1994 Mar |
Date Detail:
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Created Date: 1994-03-30 Completed Date: 1994-03-30 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0246127 Medline TA: Infect Immun Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 769-78 Citation Subset: IM |
Affiliation:
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Laboratoire de Microbiologie Génétique et Moléculaire INSERM CJF 9109, Institut Pasteur, Lille, France. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adhesins, Bacterial* Animals Bacterial Adhesion* Binding Sites Bordetella pertussis / physiology* CHO Cells Carbohydrates / pharmacology Chlorates / pharmacology Cricetinae Dextran Sulfate / metabolism, pharmacology Hela Cells Hemagglutination / drug effects Hemagglutinins / metabolism* Heparin / metabolism, pharmacology* Humans Lectins / metabolism* Oligopeptides / metabolism Virulence Factors, Bordetella* |
| Chemical | |
Reg. No./Substance:
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0/Adhesins, Bacterial; 0/Carbohydrates; 0/Chlorates; 0/Hemagglutinins; 0/Lectins; 0/Oligopeptides; 0/Virulence Factors, Bordetella; 0/filamentous hemagglutinin adhesin, Bordetella pertussis; 9005-49-6/Heparin; 9042-14-2/Dextran Sulfate; 99896-85-2/arginyl-glycyl-aspartic acid |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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