New structural insights into the multifunctional influenza A matrix protein 1
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Updated: Oct 19, 2025

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
Published on: April 21, 2015
Julia Peukes1,2, Xiaoli Xiong1,3, John A G Briggs1,4
1Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Abstract:
Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full-length M1 and show that it assembles filaments in vitro via an interface between the N- and C-terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
Insights
Influenza A virus matrix protein 1 (M1) forms filaments, revealing its structure and function in virus assembly and infection. This provides a molecular basis for understanding M1
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Influenza A virus matrix protein 1 (M1) is crucial for viral structure and replication.
- M1 protein is the most abundant protein in influenza virions.
- M1 plays key roles in nuclear RNA export, virus assembly, and disassembly.
Purpose of the Study:
- To compare and discuss the first structures of full-length M1.
- To explore the implications of M1 structures for its functions.
- To understand the molecular mechanisms of M1 in virus life cycle.
Main Methods:
- Structural analysis of full-length M1.
- Comparison of two recent M1 structure publications.
- In vitro filament assembly assays.
Main Results:
- First structures of full-length M1 reveal filament assembly via N- and C-terminal domains.
- Assembled M1 filaments resemble the virion endoskeleton.
- Structures offer molecular insights into M1's multifunctional roles.
Conclusions:
- M1 protein structures provide a molecular basis for understanding its functions.
- M1 filament formation is key to virus assembly and M1's role in infection.
- Further research can elucidate M1's interactions with viral ribonucleoproteins.
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