Publications by authors named "Aayush Bahl"
Beyond protein folding: The pleiotropic functions of PPIases in cellular processes and microbial virulence.
Biochim Biophys Acta Gen Subj
December 2024
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.
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- Trained immunity enhances innate immune responses through cellular reprogramming, differing from adaptive immunity, which relies on memory T and B cells for long-term pathogen-specific responses.
- While there's evidence supporting the concept of trained immunity and its role in personalized medicine, significant gaps remain in understanding the mechanisms and identifying specific microbial triggers.
- The review discusses infection-induced pathways in macrophages and natural killer cells, examines the biochemical basis of trained immunity, and reflects on its therapeutic potential, risks, and future research challenges.
Article Synopsis
- Mycobacterium indicus pranii (MIP) is a non-threatening bacterium that could be crucial in understanding the evolution of more harmful mycobacteria, like the Mycobacterium avium complex (MAC).
- The study investigates the previously unexplored toxin-antitoxin (TA) systems in MIP, proposing that these systems might play a role in controlling how pathogenic the bacteria can become.
- By analyzing these TA modules and comparing them to those in other bacteria, the research aims to reveal how they might affect MIP's ability to function in different environments, its virulence, and its potential use in vaccines and tuberculosis treatment.
()-encoded factors protect it against host-generated stresses and support its survival in the hostile host environment. possesses two peptidyl-prolyl isomerases and a probable trigger factor encoded by which has an FKBP-like PPIase domain. PPIases are known to assist the folding of peptidyl-prolyl bonds and are involved in various cellular processes important for bacterial survival in host-generated stresses.
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