作者: Katrin Dinkla , Manfred Rohde , Wouter T. M. Jansen , Jonathan R. Carapetis , Gursharan S. Chhatwal
DOI: 10.1046/J.1365-2958.2003.03352.X
关键词:
摘要: This study aimed to characterize matrix assembly mechanisms on the surface of human pathogen Streptococcus pyogenes. Among 125 S. pyogenes isolates, 61% were able recruit collagen type IV via surface-bound fibronectin. gordonii expressing fibronectin-binding repeat domain SfbI protein was equally potent in recruiting collagen, indicating that this sufficient promote fibronectin-mediated recruitment. Electron microscopic analysis streptococci revealed recruitment led deposition and between streptococcal cells, which induced formation large bacterial aggregates. Furthermore, collagen-recruiting colonize fibres protected from adhering polymorphonuclear cells presence opsonizing antibodies. Fibronectin-mediated thus represents a novel aggregation, colonization immune evasion mechanism