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Updated: Jan 22, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization
Ismail Dahmani1, Kai Ludwig2, Salvatore Chiantia3
1University of Potsdam, Institute of Biochemistry and Biology, Karl-Liebknecht-Str. 24-25, Potsdam 14476, Germany.
Abstract:
The matrix protein M1 of the Influenza A virus (IAV) is supposed to mediate viral assembly and budding at the plasma membrane (PM) of infected cells. In order for a new viral particle to form, the PM lipid bilayer has to bend into a vesicle toward the extracellular side. Studies in cellular models have proposed that different viral proteins might be responsible for inducing membrane curvature in this context (including M1), but a clear consensus has not been reached. In the present study, we use a combination of fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), cryo-electron tomography (cryo-ET) and scanning fluorescence correlation spectroscopy (sFCS) to investigate M1-induced membrane deformation in biophysical models of the PM. Our results indicate that M1 is indeed able to cause membrane curvature in lipid bilayers containing negatively charged lipids, in the absence of other viral components. Furthermore, we prove that protein binding is not sufficient to induce membrane restructuring. Rather, it appears that stable M1-M1 interactions and multimer formation are required in order to alter the bilayer three-dimensional structure, through the formation of a protein scaffold. Finally, our results suggest that, in a physiological context, M1-induced membrane deformation might be modulated by the initial bilayer curvature and the lateral organization of membrane components (i.e. the presence of lipid domains).
Insights
Influenza A virus matrix protein M1 induces membrane curvature essential for viral budding. Stable M1 interactions, not just binding, are key to forming a protein scaffold that deforms lipid bilayers.
Area of Science:
- Virology
- Biophysics
- Cell Biology
Background:
- The Influenza A virus (IAV) matrix protein M1 is implicated in viral assembly and budding.
- Viral budding requires bending of the host cell's plasma membrane (PM).
- The precise mechanism and viral proteins responsible for inducing membrane curvature remain debated.
Purpose of the Study:
- To investigate the role of IAV matrix protein M1 in inducing membrane deformation.
- To elucidate the biophysical mechanisms underlying M1-mediated membrane curvature in model systems.
Main Methods:
- Utilized fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), and cryo-electron tomography (cryo-ET).
- Employed scanning fluorescence correlation spectroscopy (sFCS) to analyze M1 interactions.
- Studied M1's effect on model plasma membrane lipid bilayers.
Main Results:
- Demonstrated that M1 induces membrane curvature in lipid bilayers containing negatively charged lipids.
- Showed that M1 binding alone is insufficient; stable M1-M1 interactions and multimer formation are necessary.
- Identified the formation of a protein scaffold by M1 multimers as the mechanism for bilayer restructuring.
Conclusions:
- Matrix protein M1 actively drives membrane curvature, a critical step in Influenza A virus assembly.
- M1 multimerization and scaffold formation are essential for M1-induced membrane deformation.
- Physiological membrane deformation by M1 may be influenced by initial bilayer curvature and lipid domain organization.
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