ArticleEuropean biophysics journal : EBJ2021
Towards understanding single-channel characteristics of OccK8 purified from Pseudomonas aeruginosa.
Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Design, purification, and biophysical characterization of a multi-epitope vaccine construct made from outer membrane proteins of Pseudomonas aeruginosa.Journal of computer-aided molecular design · 2026Article
- Understanding Drug Permeability inLife (Basel, Switzerland) · 2025Review
- Outer membrane permeability ofMicrobiology spectrum · 2025Article
- Revealing the single-channel characteristics of OprD (OccAB1) porins from hospital strains of Acinetobacter baumannii.European biophysics journal : EBJ · 2023Article
- Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins inProceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
6 authors at 3 institutions in 4 countries.
Funding
Abstract
Antibiotic resistance in Gram-negative bacteria causes serious health issues worldwide. Bacteria employ several resistance mechanisms to cope with antimicrobials. One of their strategies is to reduce the permeability of antibiotics either through general diffusion porins or substrate-specific channels. In this study, one of the substrate-specific channels from Pseudomonas aeruginosa, OccK8 (also known as OprE), was investigated using single-channel electrophysiology. The study also includes the investigation of permeability properties of several amino acids with different charged groups (i.e. arginine, glycine and glutamic acid) through OccK8. We observed four different conformations of the same OccK8 channel when inserted in lipid bilayers. This is in contrast to previous studies where heterologous expressed OccK8 in E. coli showed only one conformation. We hypothesized that the difference in our study was due to the expression and purification of the native channel from P. aeruginosa. The single-channel uptake characteristics of the porin showed that negatively charged glutamic acid preferentially interacted with the channel while the positively charged arginine molecule showed infrequent interaction with OccK8. The neutral amino acid glycine did not show any interaction at the physiological conditions.
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Registered trials
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