ArticleThe Journal of biological chemistry2013
Chitoporin from Vibrio harveyi, a channel with exceptional sugar specificity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 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
- Identification of anFrontiers in cellular and infection microbiology · 2025Article
- Genome analysis and hyphal movement characterization of the hitchhiker endohyphalApplied and environmental microbiology · 2024Article
- Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation.Scientific reports · 2023Article
- The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.The Journal of biological chemistry · 2021Article
- The Fish Pathogen Aliivibrio salmonicida LFI1238 Can Degrade and Metabolize Chitin despite Gene Disruption in the Chitinolytic Pathway.Applied and environmental microbiology · 2021Article
- Probing the physiological roles of the extracellular loops of chitoporin from Vibrio campbellii.Biophysical journal · 2021Article
- Structural basis of chitin utilization by a GH20 β-N-acetylglucosaminidase from Vibrio campbellii strain ATCC BAA-1116.Acta crystallographica. Section D, Structural biology · 2021Article
- Chitoporin from Serratia marcescens: recombinant expression, purification and crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- 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
- Functional analysis of an unusual porin-like channel that imports chitin for alternative carbon metabolism inThe Journal of biological chemistry · 2017Article
- Chitinase Expression in Listeria monocytogenes Is Influenced byApplied and environmental microbiology · 2017Article
- Systematic genetic dissection of chitin degradation and uptake in Vibrio cholerae.Environmental microbiology · 2017Article
- Genome-wide analyses of chitin synthases identify horizontal gene transfers towards bacteria and allow a robust and unifying classification into fungi.BMC evolutionary biology · 2016Article
- Identification and Functional Characterization of a Novel OprD-like Chitin Uptake Channel in Non-chitinolytic Bacteria.The Journal of biological chemistry · 2016Article
- Role of Electroosmosis in the Permeation of Neutral Molecules: CymA and Cyclodextrin as an Example.Biophysical journal · 2016Article
- Azide anions inhibit GH-18 endochitinase and GH-20 Exo β-N-acetylglucosaminidase from the marine bacterium Vibrio harveyi.Journal of biochemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chitoporin (VhChiP) is a sugar-specific channel responsible for the transport of chitooligosaccharides through the outer membrane of the marine bacterium Vibrio harveyi. Single channel reconstitution into black lipid membrane allowed single chitosugar binding events in the channel to be resolved. VhChiP has an exceptionally high substrate affinity, with a binding constant of K = 5.0 × 10(6) M(-1) for its best substrate (chitohexaose). The on-rates of chitosugars depend on applied voltages, as well as the side of the sugar addition, clearly indicating the inherent asymmetry of the VhChiP lumen. The binding affinity of VhChiP for chitohexaose is 1-5 orders of magnitude larger than that of other known sugar-specific porins for their preferred substrates. Thus, VhChiP is the most potent sugar-specific channel reported to date, with its high efficiency presumably reflecting the need for the bacterium to take up chitin-containing nutrients promptly under turbulent aquatic conditions to exploit them efficiently as its sole source of energy.
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