Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||M protein of the group A streptococcus binds to the seventh short consensus repeat of human complement factor H|
|Citation:||Infection and Immunity, 1998; 66(4):1427-1431|
|Publisher:||American Society for Microbiology|
|Timothy K. Blackmore, Vincent A. Fischetti, Tania A. Sadlon, Helena M. Ward, and David L. Gordon|
|Abstract:||Streptococcus pyogenes evades complement by binding the complement-regulatory protein factor H (fH) via the central conserved C-repeat region of M protein. However, the corresponding binding region within fH has not previously been precisely localized. fH is composed of 20 conserved modules called short consensus repeats (SCRs), each of which contains approximately 60 amino acids. A series of fH truncated and deletion mutants were prepared, and their interaction with M6 protein was examined. The M protein binding site was initially localized to SCRs 6 to 15 as demonstrated by ligand dot blotting, chemical cross-linking, and enzyme-linked immunosorbent assay. SCR 7 was then shown to contain the M protein binding site, as a construct consisting of the first seven SCRs bound M protein but a construct containing the first six SCRs did not bind. In addition, deletion of SCR 7 from full-length fH abolished binding to M protein. SCR 7 is known to contain a heparin binding domain, and binding of fH to M6 protein was almost totally inhibited in the presence of 400 U of heparin per ml. These results localize the M6 protein binding site of fH to SCR 7 and indicate that it is in close proximity to the heparin binding site.|
|Keywords:||CHO Cells; Animals; Humans; Streptococcus pyogenes; Heparin; Bacterial Proteins; Bacterial Outer Membrane Proteins; Complement Factor H; Carrier Proteins; Antigens, Bacterial; Binding Sites; Cricetinae|
|Rights:||Copyright © 1998 American Society for Microbiology|
|Appears in Collections:||Medical Education Unit publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.