TITLE:
AAA+ ClpB chaperone as a potential virulence factor of pathogenic microorganisms: Other aspect of its chaperone function
AUTHORS:
Joanna Krajewska, Sabina Kędzierska-Mieszkowska
KEYWORDS:
AAA+ ATPase; ClpB; Molecular Chaperone; Virulence; Pathogens
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.5 No.1,
January
8,
2014
ABSTRACT: We describe and discuss the most recent findings on
the activity and function of the oligomeric AAA+ chaperone ClpB from the
Hsp100 protein family in pathogenic 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 together with its immune reactivity suggests that ClpB acting as a protein
disaggregase may be important for pathogen invasion and virulence. However, the
specific function of ClpB in pathogenicity is still unclear. Since it is known
that ClpB does not exist in mammals, it may serve as a potential target for
the development of an effective therapy against several major bacterial
diseases that do not respond to conventional antibiotics.