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[Structure and function of the influenza virus M2 ion channel protein]
1Department of Bacteriology, Hiroshima University School of Medicine.
Abstract:
The M2 protein of influenza virus A is an integral membrane protein that is expressed on the infected cell surface and incorporated into virions. This protein is a minor component in virions but plays an essential role in the viral life cycle. The M2 protein, which forms a homotetramer, has H+ ion channel activity that is sensitive to an anti-influenza virus drug, amantadine, and is activated by low pH. When the virus enters cells, the M2 ion channel is activated in endosomes to acidify inside the virion, facilitating viral uncoating. The M2 channel also modifies the pH of the intracellular compartments to protect newly synthesized hemagglutinin from irrelevant low pH-induced conformational change for some influenza viruses.
Insights
The influenza A virus M2 protein forms an ion channel essential for viral uncoating and protecting hemagglutinin. This amantadine-sensitive channel acidifies virions after cell entry.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Context:
- Influenza A virus M2 protein is an integral membrane protein found on infected cells and virions.
- Despite being a minor component, M2 is crucial for the viral life cycle.
Purpose:
- To elucidate the function and characteristics of the influenza A virus M2 protein.
- To understand the role of the M2 ion channel in viral replication and host interactions.
Summary:
- The M2 protein forms a homotetrameric H+ ion channel, activated by low pH and inhibited by amantadine.
- Upon viral entry, the M2 channel acidifies the virion interior in endosomes, aiding viral uncoating.
- The channel also regulates intracellular pH to prevent premature hemagglutinin conformational changes.
Impact:
- Provides insights into influenza virus pathogenesis and drug resistance mechanisms.
- Highlights the M2 protein as a key target for antiviral therapies.
- Contributes to understanding host-virus interactions at the molecular level.