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BORDETELLA-PERTUSSIS FILAMENTOUS HEMAGGLUTININ INTERACTS WITH A LEUKOCYTE SIGNAL-TRANSDUCTION COMPLEX AND STIMULATES BACTERIAL ADHERENCE TO MONOCYTE CR3 (CD11B/CD18) JOURNAL OF EXPERIMENTAL MEDICINE Ishibashi, Y., Claus, S., Relman, D. A. 1994; 180 (4): 1225-1233

Abstract

Bordetella pertussis, the causative agent of whooping cough, adheres to human monocytes/macrophages by means of a bacterial surface-associated protein, filamentous hemagglutinin (FHA) and the leukocyte integrin, complement receptor 3 (CR3, alpha M beta 2, CD11b/CD18). We show that an FHA Arg-Gly-Asp site induces enhanced B. pertussis binding to monocytes, and that this enhancement is blocked by antibodies directed against CR3. Enhancement requires a monocyte signal transduction complex, composed of leukocyte response integrin (alpha? beta 3) and integrin-associated protein (CD47). This complex is known to upregulate CR3 binding activity. Thus, a bacterial pathogen enhances its own attachment to host cells by coopting a host cell signaling pathway.

View details for Web of Science ID A1994PJ70300006

View details for PubMedID 7931059