Abstract
Bacterial survival within a mammalian host is contingent upon sensing environmental perturbations and initiating an appropriate counter-response. To achieve this, sophisticated molecular machineries are used, where bacterial chaperone systems play key roles. The chaperones are a prerequisite for bacterial survival during normal physiological conditions as well as under stressful situations, e.g., infection or inflammation. Specific stress factors include, but are not limited to, high temperature, osmolarity, pH, reactive oxidative species, or bactericidal molecules. ClpB, a member of class 1 AAA+ proteins, is a key chaperone that via its disaggregase activity plays a crucial role for bacterial survival under various forms of stress, in particular heat shock. Recently, it has been reported that ClpB also regulates secretion of bacterial effector molecules related to type VI secretion systems. In this review, the roles of ClpB in stress responses and the mechanisms by which it promotes survival of pathogenic bacteria are discussed.
Highlights
AND OVERVIEWUpon infection of a host, most bacterial pathogens experience drastic changes in their environment, e.g., with regard to pH, temperature and osmolarity
Essential to these responses are the heat shock proteins (Hsps) which act as molecular chaperones to stabilize proteins and assist protein refolding under stressful conditions (Neckers and Tatu, 2008)
This review aims to elucidate our current understanding of the ClpB chaperones of pathogenic bacteria and their potential contribution to virulence
Summary
AND OVERVIEWUpon infection of a host, most bacterial pathogens experience drastic changes in their environment, e.g., with regard to pH, temperature and osmolarity. Host inflammatory responses recruit phagocytic cells, subjecting pathogens to additional adverse conditions, such as oxidative and nitrosative stresses. Bacterial survival depends on molecular adaptations, so called stress responses, to handle the adverse conditions. Essential to these responses are the heat shock proteins (Hsps) which act as molecular chaperones to stabilize proteins and assist protein refolding under stressful conditions (Neckers and Tatu, 2008). DnaJ (Hsp40), GroEL (Hsp60), DnaK (Hsp70), HtpG (Hsp90), and ClpB (Hsp100) are some of the major bacterial molecular chaperones that function in cooperation by forming complex molecular networks, thereby maintaining the overall cellular protein homeostasis (Henderson et al, 2006). ClpB is a member of the AAA+ family (ATPases associated with diverse cellular activities) that together with the DnaK system have the ability to disaggregate stress-denatured proteins. The M-domain is involved in the direct interaction of ClpB with DnaK (Haslberger et al, 2007), in the interaction of the monomer with
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