The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues

Sanderson-Smith, Martina L., Dowton, Mark, Ranson, Marie and Walker, Mark J. (2007) The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues. Journal of Bacteriology, 189 4: 1435-1440. doi:10.1128/JB.01218-06

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Author Sanderson-Smith, Martina L.
Dowton, Mark
Ranson, Marie
Walker, Mark J.
Title The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
1067-8832
Publication date 2007-02-15
Year available 2006
Sub-type Article (original research)
DOI 10.1128/JB.01218-06
Open Access Status File (Publisher version)
Volume 189
Issue 4
Start page 1435
End page 1440
Total pages 6
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted abstract
The migration of the human pathogen Streptococcus pyogenes (group A streptococcus) from localized to deep tissue sites may result in severe invasive disease, and sequestration of the host zymogen plasminogen appears crucial for virulence. Here, we describe a novel plasminogen-binding M protein, the plasminogen-binding group A streptococcal M protein (PAM)-related protein (Prp). Prp is phylogenetically distinct from previously described plasminogen-binding M proteins of group A, C, and G streptococci. While competition experiments indicate that Prp binds plasminogen with a lower affinity than PAM (50% effective concentration = 0.34 μM), Prp nonetheless binds plasminogen with high affinity and at physiologically relevant concentrations of plasminogen (Kd = 7.8 nM). Site-directed mutagenesis of the putative plasminogen binding site indicates that unlike the majority of plasminogen receptors, Prp does not interact with plasminogen exclusively via lysine residues. Mutagenesis to alanine of lysine residues Lys96 and Lys101 reduced but did not abrogate plasminogen binding by Prp. Plasminogen binding was abolished only with the additional mutagenesis of Arg107 and His108 to alanine. Furthermore, mutagenesis of Arg107 and His108 abolished plasminogen binding by Prp despite the presence of Lys96 and Lys101 in the binding site. Thus, binding to plasminogen via arginine and histidine residues appears to be a conserved mechanism among plasminogen-binding M proteins.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Published online ahead of print on 29 September 2006

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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