AAA+ ClpB chaperone as a potential virulence factor of pathogenic microorganisms: Other aspect of its chaperone function

Abstract

We describe and discuss the most recent findings on the activity and function of the oligomeric AAA+ cha-perone ClpB from the Hsp100 protein family in pa-thogenic microorganisms. Pathogens are exposed to significant stress during infection of the host cells, frequently resulting in protein aggregation. The fact that ClpB is usually up-regulated in pathogens to-gether with its immune reactivity suggests that ClpB acting as a protein disaggregase may be important for pathogen invasion and virulence. However, the spe-cific function of ClpB in pathogenicity is still unclear. Since it is known that ClpB does not exist in mam-mals, it may serve as a potential target for the devel-opment of an effective therapy against several major bacterial diseases that do not respond to conventional antibiotics.