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Updated: Jun 15, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
Published on: April 21, 2015
Influenza virus m2 ion channel protein is necessary for filamentous virion formation
Jeremy S Rossman1, Xianghong Jing, George P Leser
1Department of Biochemistry, Molecular Biology, and Cell Biology, and Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500, USA.
Abstract:
Influenza A virus buds from cells as spherical (approximately 100-nm diameter) and filamentous (approximately 100 nm x 2 to 20 microm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
Insights
The influenza A virus M2 protein
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Influenza A virus exhibits spherical and filamentous virion morphologies.
- The matrix protein M1 is known to influence viral filament formation.
- The role of the M2 integral membrane protein in filamentation is less understood.
Purpose of the Study:
- To investigate the function of the influenza virus M2 protein in viral filament formation.
- To identify specific domains within the M2 protein crucial for filamentation.
Main Methods:
- Analysis of M2 protein mutants.
- Observation of M2 protein localization during viral infection.
- Cholesterol binding assays.
Main Results:
- Specific sites within the M2 protein's cytoplasmic tail are essential for filament formation.
- M2 protein, typically a non-raft protein, localizes to lipid rafts and virus budding sites during infection.
- An amphipathic helix in the M2 cytoplasmic tail binds cholesterol.
Conclusions:
- The M2 protein's cytoplasmic tail is critical for influenza virion filamentation.
- M2 protein's ability to bind cholesterol may be vital for both forming and stabilizing viral filaments.
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