• Contribution of Streptococcus anginosus to infections caused by groups C and G streptococci, southern India.

      Reissmann, Silvana; Friedrichs, Claudia; Rajkumari, Reena; Itzek, Andreas; Fulde, Marcus; Rodloff, Arne C; Brahmadathan, Kootallur N; Chhatwal, Gursharan S; Nitsche-Schmitz, D Patric; Helmholtz Centre for Infection Research, Braunschweig, Germany. (2010-04)
      Vellore, a region in southern India, has a high incidence of severe human infections with Beta-hemolytic group C and G streptococci (GCGS). To determine the causative species in these infections, we conducted 16S rRNA gene sequencing: Streptococcus dysgalactiae subsp. equisimilis (81%) and S. anginosus (19%) were the causative organisms in the 2-year study period (2006-2007). We used PCR to detect the virulence-related emm gene; results showed that it was restricted to S. dysgalactieae subsp. equisimilis isolates of 99.2% tested positive. Due to a novel marker, S. anginosus and S. constellatus can be quickly and accurately distinguished from other members of the genus. The notable contribution of the anginosus group to human infections suggests that this group of obligate pathogens deserves more attention in healthcare and research.
    • M protein-mediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate.

      Dinkla, K; Cole, J N; Cork, A J; Maamary, P G; McArthur, J D; Chhatwal, G S; Walker, M J; School of Biological Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia. (2008-08)
      The human protease plasmin plays a crucial role in the capacity of the group A streptococcus (GAS; Streptococcus pyogenes) to initiate invasive disease. The GAS strain NS88.2 was isolated from a case of bacteremia from the Northern Territory of Australia, a region with high rates of GAS invasive disease. Mutagenesis of the NS88.2 plasminogen binding M protein Prp was undertaken to examine the contribution of plasminogen binding and cell surface plasmin acquisition to virulence. The isogenic mutant NS88.2prp was engineered whereby four amino acid residues critical for plasminogen binding were converted to alanine codons in the GAS genome sequence. The mutated residues were reverse complemented to the wild-type sequence to construct GAS strain NS88.2prpRC. In comparison to NS88.2 and NS88.2prpRC, the NS88.2prp mutant exhibited significantly reduced ability to bind human plasminogen and accumulate cell surface plasmin activity during growth in human plasma. Utilizing a humanized plasminogen mouse model of invasive infection, we demonstrate that the capacity to bind plasminogen and accumulate surface plasmin activity plays an essential role in GAS virulence.