ArticleJournal of virology2017
Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Continuum and discrete modeling of binding-site distribution-mediated reactions on lipid surfaces.Biophysical journal · 2026Article
- Asymmetry and heterogeneity in the plasma membrane.Biophysical journal · 2026Article
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- Visualizing influenza A virus assembly by in situ cryo-electron tomography.Nature communications · 2025Article
- Molecular patterns of matrix protein 1 (M1): A strong predictor of adaptive evolution in H9N2 avian influenza viruses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A physical model for M1-mediated influenza A virus assembly.Biophysical journal · 2025Article
- Review
- Influenza A Virus Infection Alters Lipid Packing and Surface Electrostatic Potential of the Host Plasma Membrane.Viruses · 2023Article
- Graph-Based Analyses of Dynamic Water-Mediated Hydrogen-Bond Networks in Phosphatidylserine: Cholesterol Membranes.Biomolecules · 2023Article
- Structural Insights into the Mechanism of HIV-1 Tat Secretion from the Plasma Membrane.Journal of molecular biology · 2023Article
- Influenza A Virus M1 Protein Non-Specifically Deforms Charged Lipid Membranes and Specifically Interacts with the Raft Boundary.Membranes · 2023Article
- Article
- Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.EMBO reports · 2022Article
- Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.Science advances · 2022Article
- Review
- Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- Influenza A virus hemagglutinin prevents extensive membrane damage upon dehydration.BBA advances · 2022Article
- Influenza A M2 recruits M1 to the plasma membrane: A fluorescence fluctuation microscopy study.Biophysical journal · 2021Article
- Article
- Negative-sense RNA viruses: An underexplored platform for examining virus-host lipid interactions.Molecular biology of the cell · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus matrix protein 1 (M1) is an essential component involved in the structural stability of the virus and in the budding of new virions from infected cells. A deeper understanding of the molecular basis of virion formation and the budding process is required in order to devise new therapeutic approaches. We performed a detailed investigation of the interaction between M1 and phosphatidylserine (PS) (i.e., its main binding target at the plasma membrane [PM]), as well as the distribution of PS itself, both in model membranes and in living cells. To this end, we used a combination of techniques, including Förster resonance energy transfer (FRET), confocal microscopy imaging, raster image correlation spectroscopy, and number and brightness (N&B) analysis. Our results show that PS can cluster in segregated regions in the plane of the lipid bilayer, both in model bilayers constituted of PS and phosphatidylcholine and in living cells. The viral protein M1 interacts specifically with PS-enriched domains, and such interaction in turn affects its oligomerization process. Furthermore, M1 can stabilize PS domains, as observed in model membranes. For living cells, the presence of PS clusters is suggested by N&B experiments monitoring the clustering of the PS sensor lactadherin. Also, colocalization between M1 and a fluorescent PS probe suggest that, in infected cells, the matrix protein can specifically bind to the regions of PM in which PS is clustered. Taken together, our observations provide novel evidence regarding the role of PS-rich domains in tuning M1-lipid and M1-M1 interactions at the PM of infected cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.