Structural and functional analysis of RopB: a major virulence regulator in Streptococcus pyogenes.

ABSTRACT: Group A Streptococcus (GAS) is an exclusive human pathogen that causes significant disease burden. Global regulator RopB of GAS controls the expression of several major virulence factors including secreted protease SpeB during high cell density. However, the molecular mechanism for RopB-dependent speB expression remains unclear. To understand the mechanism of transcription activation by RopB, we determined the crystal structure of the C-terminal domain of RopB. RopB-CTD has the TPR motif, a signature motif involved in protein-peptide interactions and shares significant structural homology with the quorum sensing RRNPP family regulators. Characterization of the high cell density-specific cell-free growth medium demonstrated the presence of a low molecular weight proteinaceous secreted facto

SUBMITTER: Makthal N 

PROVIDER: S-EPMC4794775 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature