Beyond protein folding: The pleiotropic functions of PPIases in cellular processes and microbial virulence.

Peptidyl prolyl cis/trans isomerases (PPIases), a ubiquitously distributed superfamily of enzymes, associated with signal transduction, trafficking, assembly, biofilm formation, stress tolerance, cell cycle regulation, gene expression and tissue regeneration, is a key regulator of metabolic disorders and microbial virulence. This review assumes an integrative approach, to provide a holistic overview of the structural and functional diversity of PPIases, examining their conformational dynamics, cellular distribution, and physiological significance. We explore their intricate involvement in cellular processes and virulence modulation in both eukaryotic and prokaryotic systems. Additionally, we evaluate the potential of these molecular chaperones as drug targets and vaccine candidates, emphasizing their relevance in therapeutic development. By synthesizing recent findings and providing a broader perspective on these proteins, this review aims to enhance our understanding of their multifaceted roles in biology and their potential applications in medicine. Copyright © 2024. Published by Elsevier B.V.

Citation

Roopshali Rakshit, Aayush Bahl, Arunima Arunima, Saurabh Pandey, Deeksha Tripathi. Beyond protein folding: The pleiotropic functions of PPIases in cellular processes and microbial virulence. Biochimica et biophysica acta. General subjects. 2025 Feb;1869(2):130754

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PMID: 39732207

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