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August 13, 2026Proteins Structure Function and Bioinformatics

Protonation Based Molecular Mechanism Behind Rv0191 Efflux Transporter Conferring Pyrazinamide Resistance in Mycobacterium tuberculosis

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Authors

DDDeepti DhusiaBabasaheb Bhimrao Ambedkar UniversityGSGarima SinghBabasaheb Bhimrao Ambedkar UniversityDMDinesh Raj ModiBabasaheb Bhimrao Ambedkar University

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Overview

Randomized trial explores drug efflux mechanism in Mycobacterium tuberculosis, suggesting new therapeutic targets.

Key Points

  • This research investigates the molecular mechanisms of Rv0191 efflux transporter related to pyrazinamide resistance in Mycobacterium tuberculosis.
  • Studied two conformations of Rv0191: outward-open (protonated) and inward-open (unprotonated) for drug efflux analysis.
  • Conducted 500 ns of molecular dynamics simulations on the PZA-docked structure within a lipid bilayer.
  • Analyzed specific interactions and conformational changes of Rv0191 during substrate transport.
  • The efflux process was facilitated by a protonation-driven mechanism, highlighting functional differences between conformations.
  • Distinct interactions between pyrazinamide and the Rv0191 binding pocket were observed during simulations.
  • Conformational dynamics indicated a potential pathway for pyrazinamide translocation from the cytoplasm to the periplasm.

Cite This Study

Dhusia et al. (2026) studied this question.

synapsesocial.com/papers/6a7d768a2b0e0cff3f63fee7https://doi.org/10.1002/prot.70165
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