Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Viral ion channels: structure and function.

Wolfgang B Fischer1, Mark S P Sansom

  • 1Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, UK. wolfgang.fischer@bioch.ox.ac.uk

Biochimica Et Biophysica Acta
|May 4, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Insights from aquaporin structures into drug-resistant sleeping sickness.

eLife·2026
Same author

Electronic Polarizability Tunes the Function of the Human Bestrophin 1 Cl<sup>-</sup> Channel.

Journal of chemical theory and computation·2025
Same author

Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery.

Nature reviews. Drug discovery·2025
Same author

The Role of Cholesterol in M2 Clustering and Viral Budding Explained.

Journal of chemical theory and computation·2024
Same author

Molecular mechanism of anion permeation through aquaporin 6.

Biophysical journal·2024
Same author

Mapping structural and dynamic divergence across the MBOAT family.

Structure (London, England : 1993)·2024
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

This review explores viral ion channels, including M2, NB, CM2, and Vpu proteins, found in viruses like influenza and HIV-1. These miniaturized membrane proteins form oligomers to facilitate ion transport, with ongoing research into their structure, function, and drug interactions.

Area of Science:

  • Virology
  • Structural Biology
  • Membrane Biophysics

Background:

  • Viral ion channels are small auxiliary membrane proteins crucial for viral function.
  • Examples include M2 (Influenza A), NB (Influenza B), CM2 (Influenza C), and Vpu (HIV-1).
  • A potassium-selective ion channel has also been identified in Paramecium bursaria chlorella virus (PBCV-1).

Purpose of the Study:

  • To summarize current knowledge on short viral membrane proteins.
  • To outline the discovery and discuss experimental evidence for their structure and function.
  • To present computational studies and drug-protein interaction investigations.

Main Methods:

  • Review of existing literature on viral ion channels.
  • Analysis of experimental data regarding structure and function.

Related Experiment Videos

  • Inclusion of computational modeling and drug interaction studies.
  • Main Results:

    • Viral ion channels form homo-oligomers to enable ion flux.
    • Proton conductivity is established for M2; NB, Vpu, and PBCV-1 channel conduct ions.
    • Ion conductivity for CM2 is under investigation.

    Conclusions:

    • Short viral membrane proteins represent miniaturized systems with diverse ion transport capabilities.
    • Understanding their structure and function is key for therapeutic development.
    • Further research is needed, particularly for CM2 ion conductivity.