| dc.description.abstract | The Clp/Hsp100 family, part of the ATPase associated with various
cellular activities (AAA+) superfamily, includes caseinolytic
peptidase B (ClpB), a highly conserved protein found in bacteria,
fungi, protozoa, and plants. Notably, ClpB is present in all ESKAPE
pathogens: Enterococcus faecium, Staphylococcus aureus, Klebsiella
pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa,
and Enterobacter spp. ClpB plays a crucial role in reactivating
and disaggregating proteins, enabling pathogens to survive under
host-induced stress and conferring thermotolerance to bacterial
cells. Infections caused by ESKAPE pathogens are particularly
challenging due to their resistance to broad-spectrum antibiotics and
biofilm formation, posing a significant global health threat as they
are often multidrug-resistant, extensively drug-resistant, and pan drug-resistant. Given its absence in human cells and its essential
role in bacterial survival under stress, ClpB is a promising target
for antimicrobial therapy. Targeting Hsp100 family proteins could
lead to the development of novel antifungal and antiprotozoal
treatments. This review explores the function of ClpB in the survival
of ESKAPE pathogens and the protozoan Plasmodium falciparum.
Relevant research findings were compiled using academic databases,
and data analysis was performed using Clustal Omega Multiple
Sequence Alignment and Boxshade tools. | en_US |
