Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18).
J Exp Med
; 180(4): 1225-33, 1994 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-7931059
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aderência Bacteriana
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Bordetella pertussis
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Fatores de Virulência de Bordetella
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Monócitos
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Transdução de Sinais
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Antígeno de Macrófago 1
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Adesinas Bacterianas
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Hemaglutininas
Limite:
Humans
Idioma:
En
Revista:
J Exp Med
Ano de publicação:
1994
Tipo de documento:
Article