The ClpXP protease and the ClpX unfoldase control virulence, cell division, and autolysis in <i>Streptococcus pneumoniae</i>.

ABSTRACT: In all living cells, molecular chaperones and ATP-dependent proteases are essential for protein homeostasis. The ClpXP protease is a chaperone-protease complex conserved between bacteria and mitochondria. Proteolytic activity resides in the caseinolytic protease (ClpP) subunits that associate to form a tetradecameric serine protease that degrades substrates recognized and unfolded by the ClpX ATPase. In the important human pathogen Streptococcus pneumoniae (Spn), ClpX but not ClpP was proposed to be essential for viability. We here follow up on this finding by characterizing phenotypes associated with depriving S. pneumoniae D39V of ClpX unfoldase or ClpXP activity. Virulence was examined in the Galleria melonella infection model and was found to be severely att

SUBMITTER: Mebus VH 

PROVIDER: S-EPMC12211083 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature