ArticleBiochimica et biophysica acta. Biomembranes2021
An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.
Article in Biochimica et biophysica acta. Biomembranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Molecular basis of ampicillin resistance: combinatorial mechanisms and future strategies.World journal of microbiology & biotechnology · 2026Review
- Understanding Drug Permeability inLife (Basel, Switzerland) · 2025Review
- Isolation of human monoclonal antibodies from 4CMenB vaccinees reveals PorB and LOS as the main OMV components inducing cross-strain protection.Frontiers in immunology · 2025Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Multidrug efflux in Gram-negative bacteria: structural modifications in active compounds leading to efflux pump avoidance.npj antimicrobials and resistance · 2024Article
- An insights into emerging trends to control the threats of antimicrobial resistance (AMR): an address to public health risks.Archives of microbiology · 2024Review
- Affinity Purification of Membrane β-Barrel Proteins via Biotin-Tagged Peptidiscs.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The Influence of Outer Membrane Protein on Ampicillin Resistance ofThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2023Article
- Data-Driven Derivation of Molecular Substructures That Enhance Drug Activity in Gram-Negative Bacteria.Journal of medicinal chemistry · 2022Article
- Analysis of patchclamp recordings: model-free multiscale methods and software.European biophysics journal : EBJ · 2021Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
Gram-negative bacteria cause the majority of highly drug-resistant bacterial infections. To cross the outer membrane of the complex Gram-negative cell envelope, antibiotics permeate through porins, trimeric channel proteins that enable the exchange of small polar molecules. Mutations in porins contribute to the development of drug-resistant phenotypes. In this work, we show that a single point mutation in the porin PorB from Neisseria meningitidis, the causative agent of bacterial meningitis, can strongly affect the binding and permeation of beta-lactam antibiotics. Using X-ray crystallography, high-resolution electrophysiology, atomistic biomolecular simulation, and liposome swelling experiments, we demonstrate differences in drug binding affinity, ion selectivity and drug permeability of PorB. Our work further reveals distinct interactions between the transversal electric field in the porin eyelet and the zwitterionic drugs, which manifest themselves under applied electric fields in electrophysiology and are altered by the mutation. These observations may apply more broadly to drug-porin interactions in other channels. Our results improve the molecular understanding of porin-based drug-resistance in Gram-negative bacteria.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.