The Plasminogen-Binding Group A Streptococcal M Protein-Related Protein Prp Binds Plasminogen via Arginine and Histidine Residues
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This article was originally published as Sanderson-Smith, ML, Dowton, M, Ranson, M and Walker, MJ, The Plasminogen-Binding Group A Streptococcal M Protein-Related Protein Prp Binds Plasminogen via Arginine and Histidine Residues, Journal
phylogenetically distinct from previously described plasminogen-binding M proteins of Lys96 and Lys101 in the putative plasminogen binding site indicates that Prp binds plasminogen with a The migration of plasminogen receptors, Prp does not interact with plasminogen exclusively via lysine residues. Mutagenesis to alanine. Furthermore, mutagenesis of lysine residues Lys96 and Lys101 reduced but did not abrogate plasminogen binding by Prp. Plasminogen binding was abolished only with the conserved mechanism among plasminogen-binding M proteins. a novel plasminogen-binding M protein, the presence of plasminogen (Kd = 7.8 nM). Site-directed mutagenesis of the host zymogen plasminogen appears crucial for virulence. Here, we describe a lower affinity than PAM (50% effective concentration = 0.34 µM), Prp nonetheless binds plasminogen with high affinity and at physiologically relevant concentrations of alanine of the majority of Arg107 and His108 abolished plasminogen binding is Prp despite the human pathogen Streptococcus pyogenes (group A streptococcus) from localized to be of group A, C, and G streptococci. While competition experiments indicate that additional mutagenesis of Arg107 and His108 to deep tissue sites may result in severe invasive disease, and sequestration by the binding site. Thus, binding to plasminogen via arginine and histidine residues appears to unlike the plasminogen-binding group A streptococcal M protein (PAM)-related protein (Prp). Prp
