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Group A streptococcal growth phase‐associated virulence factor regulation by a novel operon (Fas) with homologies to two‐component‐type regulators requires a small RNA molecule
Despite structural and functional similarities between fas and agr, to date the fas operon appears not to be involved in group A streptococcal (GAS) quorum‐sensing regulation.
M‐related protein (Mrp) contributes to group A streptococcal resistance to phagocytosis by human granulocytes
Analysis of phagocytosis by flow cytometry andKinetic data suggested that attachment to granulocytes proceeds faster for emm mutants than for corresponding mrp mutants, which indicated that, if present, both mrP and emm gene products contribute to phagcytosis resistance by decreasing bacterial binding togranulocytes.
Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor
The deduced amino acid sequence for the plasmin receptor protein revealed significant similarity (39 to 54% identical amino acid residues) to glyceraldehyde 3-phosphate dehydrogenases.
Plasminogen activation by invasive human pathogens.
Evidence is presented for multiple mechanisms by which human pathogens can acquire a surface bound form of plasmin that cannot be regulated by host serpins.
Nephritis-associated plasmin receptor and acute poststreptococcal glomerulonephritis: characterization of the antigen and associated immune response.
The role of nephritis-associated antigen as a virulence factor for acute poststreptococcal glomerulonephritis (APSGN) remains to be fully clarified and antibody titers remained elevated during the entire 10-yr follow-up period.
Identification of pel, aStreptococcus pyogenes Locus That Affects both Surface and Secreted Proteins
Characterization of the pel mutant provides evidence for the coordinated regulation of secreted and surface proteins and suggests the existence of a new global regulatory factor in S. pyogenes.
The potential role for nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis.
It is speculated that NAPlr bound to the glomeruli may contribute to the pathogenesis of APSGN via plasmin and complement activation.