Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18).
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.
Ishibashi
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Y
Department of Microbiology and Immunology, Stanford University School of Medicine, California 94305.
Claus
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Relman
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D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion; D001483:Base Sequence; D001886:Bordetella pertussis / Q000502:physiology*; D006388:Hemagglutinins / Q000502:physiology*; D006801:Humans; D016177:Macrophage-1 Antigen / Q000502:physiology*; D008969:Molecular Sequence Data; D009000:Monocytes / Q000382:microbiology*; D009842:Oligopeptides / Q000502:physiology; D017469:Receptors, Fibronectin / Q000502:physiology; D015398:Signal Transduction; D010566:Virulence Factors, Bordetella
D018829:Adhesins, Bacterial; D006388:Hemagglutinins; D016177:Macrophage-1 Antigen; D009842:Oligopeptides; D017469:Receptors, Fibronectin; D010566:Virulence Factors, Bordetella; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; C047981:arginyl-glycyl-aspartic acid