ArticleThe Journal of biological chemistry2015
Chitoporin from the Marine Bacterium Vibrio harveyi: PROBING THE ESSENTIAL ROLES OF TRP136 AT THE SURFACE OF THE CONSTRICTION ZONE.
Article in The Journal of biological chemistry, 2015. 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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10 citing papers in PubMed, 19 citations in OpenAlex.
- Structure-based classification of bacterial chitooligosaccharide-specific outer membrane porins (ChiPs).The Journal of biological chemistry · 2026Article
- Functional genomics of chitin degradation by Vibrio parahaemolyticus reveals finely integrated metabolic contributions to support environmental fitness.PLoS genetics · 2025Article
- Genome analysis and hyphal movement characterization of the hitchhiker endohyphalApplied and environmental microbiology · 2024Article
- Genomic analysis and chitinase characterization ofFrontiers in microbiology · 2023Article
- The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.The Journal of biological chemistry · 2021Article
- Probing the physiological roles of the extracellular loops of chitoporin from Vibrio campbellii.Biophysical journal · 2021Article
- Single-channel properties, sugar specificity, and role of chitoporin in adaptive survival ofThe Journal of biological chemistry · 2020Article
- Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marineThe Journal of biological chemistry · 2018Article
- Structural basis for chitin acquisition by marine Vibrio species.Nature communications · 2018Article
- Identification and Functional Characterization of a Novel OprD-like Chitin Uptake Channel in Non-chitinolytic Bacteria.The Journal of biological chemistry · 2016Article
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5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VhChiP is a sugar-specific porin present in the outer membrane of the marine bacterium Vibrio harveyi. VhChiP is responsible for the uptake of chitin oligosaccharides, with particular selectivity for chitohexaose. In this study, we employed electrophysiological and biochemical approaches to demonstrate that Trp(136), located at the mouth of the VhChiP pore, plays an essential role in controlling the channel's ion conductivity, chitin affinity, and permeability. Kinetic analysis of sugar translocation obtained from single channel recordings indicated that the Trp(136) mutations W136A, W136D, W136R, and W136F considerably reduce the binding affinity of the protein channel for its best substrate, chitohexaose. Liposome swelling assays confirmed that the Trp(136) mutations decreased the rate of bulk chitohexaose permeation through the VhChiP channel. Notably, all of the mutants show increases in the off-rate for chitohexaose of up to 20-fold compared with that of the native channel. Furthermore, the cation/anion permeability ratio Pc/Pa is decreased in the W136R mutant and increased in the W136D mutant. This demonstrates that the negatively charged surface at the interior of the protein lumen preferentially attracts cationic species, leading to the cation selectivity of this trimeric channel.
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