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. 1994 Mar;62(3):769–778. doi: 10.1128/iai.62.3.769-778.1994

Heparin-inhibitable lectin activity of the filamentous hemagglutinin adhesin of Bordetella pertussis.

F D Menozzi 1, R Mutombo 1, G Renauld 1, C Gantiez 1, J H Hannah 1, E Leininger 1, M J Brennan 1, C Locht 1
PMCID: PMC186182  PMID: 8112848

Abstract

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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Selected References

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