Biological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis

Abstract

CitationBiological functions of GCS3, a novel plasminogen-

Bacterial Plasminogen Receptors: Mediators of a Multifaceted Relationship

“…Recently, a plasminogen-binding M protein expressed by the group G streptococci S. canis was reported to bind to miniplasminogen, a plasminogen variant consisting of only K5 and the serine protease domain [28]. Similarly, the M-like protein of group C streptococcus GCS3 likely interacts with K4 or K5 of plasminogen [40]. K4 and K5 show a high affinity for lysine-based ligands when compared with K2 [8], so, whilst specific plasminogen-binding sites within the M proteins of group C streptococcus and S. canis are yet to be defined, it is likely that they display markedly different properties to the internal motif described for the group A streptococcal plasminogen-binding M proteins.…”

“…When this bridging plasminogen molecule is activated by tPA to plasmin, it can digest intercellular junctions and disrupt cell monolayers in ECM models [137]. Similarly, the streptococcal M protein GSC3 has been shown to mediate plasminogen-dependant adherence of streptococci to pharyngeal cells [40], implying a role for plasminogen binding in colonisation of the throat and oral cavity by bacteria. A role for plasminogen binding in colonisation has been further demonstrated for S. pyogenes interaction with keratinocytes.…”

Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system

“…Based on this, three groups of proteins can be assigned (Table 1 ): (a) the M- and M-like proteins of pyogenic streptococci, e.g., S. canis , GAS, and S. dysgalactiae subs. equisimilis ( S. equisimilis ) represent a first group (Berge and Sjöbring, 1993 ; Sanderson-Smith et al, 2006a , b ; Bergmann et al, 2011 ; Fulde et al, 2011 , 2013a ). These proteins harbor a fibrillar structure with the tendency to dimerize and are covalently linked to the bacterial cell wall via a typical LPxTG motif (Fischetti, 1991 ).…”

“…In 1995; Wistedt and co-workers identified K2 as the interaction site of the GAS M Protein PAM (Table 1 ) (Wistedt et al, 1995 ). In contrast, SCM, a M-like protein of S. canis , and the M protein GCS3 of S. equisimilis interact with mPLG (Table 1 ) (Bergmann et al, 2011 ; Fulde et al, 2011 , 2013a ). (b) The second group includes several enzymes of the glycolytic pathway like enolase, phosphoglycerate kinase (PGK), and glyceraldhehyde-3-phosphate-dehydrogenase (GAPDH), a surface dehydrogenase (SDH).…”

Host-Pathogen Interactions in Streptococcal Diseases

“…Interestingly, only two respective genes were detected, slo and emm (DeWinter et al 1999). S. zooepidemicus and S. iniae (Baiano et al 2008(Baiano et al , 2009Bergmann et al 2011;Meehan et al 2001;Nitsche-Schmitz et al 2007;Nitsche et al 2006;Timoney et al 1997Timoney et al , 2010, bind extracellular matrix (ECM) and serum proteins. SAgs are phage-encoded virulence factors extensively studied in GAS.…”