ArticleAntimicrobial agents and chemotherapy2000
Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel.
Article in Antimicrobial agents and chemotherapy, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 79 citations in OpenAlex.
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- Outer membrane permeability ofMicrobiology spectrum · 2025Article
- Guiding the Way: Traditional Medicinal Chemistry Inspiration for Rational Gram-Negative Drug Design.Journal of medicinal chemistry · 2024Review
- Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C β-Lactamases.Antimicrobial agents and chemotherapy · 2023Article
- Avian PathogenicVeterinary sciences · 2022Article
- Role of internal loop dynamics in antibiotic permeability of outer membrane porins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB.Scientific reports · 2019Article
- Mechanisms of Bacterial Resistance to Antimicrobial Agents.Microbiology spectrum · 2018Article
- The fitness costs and trade-off shapes associated with the exclusion of nine antibiotics by OmpF porin channels.The ISME journal · 2017Article
- YgaE regulates out membrane proteins in Salmonella enterica serovar Typhi under hyperosmotic stress.TheScientificWorldJournal · 2014Article
- Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The binding of antibiotics in OmpF porin.Structure (London, England : 1993) · 2013Article
- Structure, Function and Regulation of Outer Membrane Proteins Involved in Drug Transport in Enterobactericeae: the OmpF/C - TolC Case.The open microbiology journal · 2013Article
- Microbe-host interactions: structure and role of Gram-negative bacterial porins.Current protein & peptide science · 2012Review
- Bridging timescales and length scales: from macroscopic flux to the molecular mechanism of antibiotic diffusion through porins.Biophysical journal · 2010Article
- Outer membrane permeability and antibiotic resistance.Biochimica et biophysica acta · 2009Review
- Article
- Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli OmpF porin is a nonspecific channel involved in the membrane translocation of small hydrophilic molecules and especially in the passage of beta-lactam antibiotics. In order to understand the dynamic of charged-compound uptake through bacterial porins, specific charges located in the E. coli OmpF channel were mutated. Substitutions G119D and G119E, inserting a protruding acidic side chain into the pore, decreased cephalosporin and colicin susceptibilities. Cefepime diffusion was drastically altered by these mutations. Conversely, substitutions R132A and R132D, changing a residue located in the positively charged cluster, increased the rate of cephalosporin uptake without modifying colicin sensitivity. Modelling approaches suggest that G119E generates a transverse hydrogen bond dividing the pore, while the two R132 substitutions stretch the channel size. These charge alterations located in the constriction area have differential effects on cephalosporin diffusion and substantially modify the profile of antibiotic susceptibility.
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