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

Current Microbiology
Harry S CourtneyDavid L Hasty

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 beta 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.

Citations

Sep 2, 2009·Microbiology and Molecular Biology Reviews : MMBR·Angela H NobbsHoward F Jenkinson
Sep 5, 2007·Molecular Immunology·Peter F ZipfelChristine Skerka
Mar 8, 2005·Journal of Thrombosis and Haemostasis : JTH·L R Zacharski, V P Sukhatme
Jan 20, 2006·Molecular Microbiology·Harry S CourtneyJames B Dale
Sep 1, 2006·Molecular Microbiology·Anjuli M TimmerVictor Nizet
Mar 20, 2015·Frontiers in Cellular and Infection Microbiology·Yaya PianYongqiang Jiang
Jun 18, 2016·FEBS Letters·Stephan BrouwerMark J Walker
Feb 17, 2017·Journal of the Pediatric Infectious Diseases Society·Nicholas D HysmithJames B Dale
Aug 7, 2021·Frontiers in Cardiovascular Medicine·M Taariq SalieMark E Engel

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