Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Influenza

Influenza

Influenza is an acute, highly communicable viral disease that affects the respiratory tract and is responsible for seasonal epidemics worldwide. Influenza A is the most prevalent type associated with widespread outbreaks and is subtyped based on two surface glycoproteins: hemagglutinin (H) and neuraminidase (N), as in H1N1. These glycoproteins are essential for viral infectivity, transmission, and immune recognition. Transmission occurs primarily through respiratory droplets and contaminated...

Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

Inhibitors Of Virion Release

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...

G-Protein Gated Ion Channels

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...

Non-gated Ion Channels

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.

Non-gated Ion Channels

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.

You might also read

Related Articles

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

Sort by

Same author

A ligandable PNT domain establishes ERG as a directly targetable oncogenic driver in prostate cancer.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Void-X: A generative void-filling model for predicting atomic packing in proteins.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Structural rewiring of IL-7R dimerization by an oncogenic transmembrane mutation can be reversed by rational design.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Electric dipole moment drives the dynamics of the TNFR1 complex I signalosome.

Nature·2026

Same author

Repression of RIPK1 kinase by INPP5D inhibits expression of diverse proinflammatory mediators and late-onset Alzheimer's disease risk factors.

Immunity·2026

Same author

A comprehensive proteome structural analysis suggests undiscovered functional domains in ocean archaea.

Protein science : a publication of the Protein Society·2025

Search research articles

Related Experiment Video

Updated: Jun 13, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Published on: April 21, 2015

Influenza M2 proton channels.

Rafal M Pielak¹, James J Chou

¹Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

Biochimica Et Biophysica Acta

|May 11, 2010

Summary

This summary is machine-generated.

The influenza virus M2 protein forms a proton channel crucial for viral replication. Recent structural studies reveal how this channel conducts protons and how drugs like amantadine work.

More Related Videos

Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals

Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals

Published on: April 15, 2017

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells

Published on: June 3, 2012

Related Experiment Videos

Last Updated: Jun 13, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Published on: April 21, 2015

Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals

Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals

Published on: April 15, 2017

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells

Published on: June 3, 2012

Area of Science:

Virology
Structural Biology
Biophysics

Background:

The M2 protein of the influenza virus forms a proton channel essential for viral replication.
This channel plays a key role in viral entry and maturation by regulating pH.
M2 protein is a target for antiviral drugs such as amantadine and rimantadine.

Purpose of the Study:

To review the current understanding of proton conduction through the influenza M2 channel.
To summarize structural insights into the M2 proton channel mechanism.
To elucidate the function of gating elements in M2 channel activity.

Main Methods:

High-resolution structural determination of M2 channels from influenza A and B.
Utilizing functional solution Nuclear Magnetic Resonance (NMR) systems.
Simultaneous characterization of channel structure, dynamics, and activity.

Main Results:

High-resolution structures of M2 channels from influenza A and B have been obtained.
Functional solution NMR systems allow coupled structure and dynamics measurements.
Insights into the mechanism of proton conductance and channel gating have been gained.

Conclusions:

Structural and dynamic studies provide a detailed understanding of M2 proton channel function.
Understanding the M2 channel mechanism is crucial for developing new antiviral strategies.
The M2 channel's gating elements are key to its role in proton conduction.