A physical model for M1-mediated influenza A virus assembly
Influenza A virus particles assemble at the plasma membrane of infected cells. During assembly all components of the virus come together in a coordinated manner to deform the membrane into a protrusion eventually forming a new, membrane-enveloped virus. Here, we integrate recent molecular insights of this process, particularly concerning the structure of the matrix protein 1 (M1), within a theoretical framework describing the mechanics of virus assembly. Our model describes M1 polymerization and membrane protrusion formation, explaining why it is efficient for M1 to form long strands assembling into helices in filamentous virions. Eventually, we find how the architecture of M1 helices is controlled by physical properties of viral proteins and the host cell membrane. Finally, by considering the growth force and speed of viral filaments, we propose that the helical geometry of M1 strands might have evolved to optimize for fast and efficient virus assembly and growth.
Authors
- John A. G. Briggs (ORCID: https://orcid.org/0000-0003-3990-6910)
- Julia Peukes (ORCID: https://orcid.org/0000-0001-8560-7407)
- Serge Dmitrieff (ORCID: https://orcid.org/0000-0002-1362-5670)
- François Nédélec (ORCID: https://orcid.org/0000-0002-8141-5288)
Institutions
- QB3 (US)
- Université Paris Cité (FR)
- University of Cambridge (GB)
- Sainsbury Laboratory (GB)
- Institut Jacques Monod (FR)
- Max Planck Institute of Biochemistry (DE)
Publication Details
- Journal
- Biophysical Journal
- Published
- 2024-11-20
- DOI
- https://doi.org/10.1016/j.bpj.2024.11.016
- Citations
- 2
- Primary Topic
- Influenza Virus Research Studies
- Type
- article
- Field-Weighted Citation Impact
- 0.77
Funders
- European Molecular Biology Laboratory
- Max-Planck-Gesellschaft
- Centre National de la Recherche Scientifique
- Medical Research Council