Streptococcus pyogenes recruits collagen via surface-bound fibronectin: a novel colonization and immune evasion mechanism.
Mol Microbiol
; 47(3): 861-9, 2003 Feb.
Article
en En
| MEDLINE
| ID: mdl-12535082
ABSTRACT
This study aimed to characterize matrix assembly mechanisms on the surface of the human pathogen Streptococcus pyogenes. Among 125 S. pyogenes isolates, 61% were able to recruit collagen type IV via surface-bound fibronectin. Streptococcus gordonii expressing the fibronectin-binding repeat domain of S. pyogenes SfbI protein was equally potent in recruiting collagen, indicating that this domain was sufficient to promote fibronectin-mediated collagen recruitment. Electron microscopic analysis of streptococci revealed that fibronectin-mediated collagen recruitment led to matrix deposition on and between streptococcal cells, which induced the formation of large bacterial aggregates. Furthermore, collagen-recruiting streptococci were able to colonize collagen fibres and were protected from adhering to human polymorphonuclear cells in the presence of opsonizing antibodies. Fibronectin-mediated collagen recruitment thus represents a novel aggregation, colonization and immune evasion mechanism of S. pyogenes.
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Bases de datos:
MEDLINE
Asunto principal:
Streptococcus pyogenes
/
Proteínas Bacterianas
/
Adhesión Bacteriana
/
Proteínas Portadoras
/
Colágeno
/
Fibronectinas
/
Adhesinas Bacterianas
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Mol Microbiol
Asunto de la revista:
BIOLOGIA MOLECULAR
/
MICROBIOLOGIA
Año:
2003
Tipo del documento:
Article
País de afiliación:
Alemania