Mapping the fibrinogen-binding domain of serum opacity factor of group A streptococci

Harry Courtney, James Dale, David L. Hasty

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Serum opacity factor (SOF) is a large, extracellular, and cell-bound protein of group A streptococci that has two known functions, opacification of serum and binding of fibronectin. Herein, we describe a new function of SOF, the binding of fibrinogen. Utilizing purified, truncated recombinant SOF proteins, the fibrinogen-binding domain was localized to a region in the C-terminus of SOF encompassing amino acid residues 844-1047. Western-blot analysis revealed that SOF bound primarily to the β subunit of fibrinogen. A SOF-negative mutant bound 50% less fibrinogen than did its wild-type parent. Furthermore, fibrinogen blocked the binding of SOF to fibronectin. These data suggest that fibrinogen and fibronectin bind to the same domain within SOF. It remains to be determined whether the binding of fibrinogen to SOF contributes to the virulence of group A streptococci.

Original languageEnglish (US)
Pages (from-to)236-240
Number of pages5
JournalCurrent Microbiology
Volume44
Issue number4
DOIs
StatePublished - Apr 1 2002

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Streptococcus
Fibrinogen
Fibronectins
opacity factor
Protein Binding
Virulence
Western Blotting
Amino Acids
Serum

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

Cite this

Mapping the fibrinogen-binding domain of serum opacity factor of group A streptococci. / Courtney, Harry; Dale, James; Hasty, David L.

In: Current Microbiology, Vol. 44, No. 4, 01.04.2002, p. 236-240.

Research output: Contribution to journalArticle

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