ArticleScientific reports2017
Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- 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
- Review
- HIV-1 Gag Polyprotein Affinity to the Lipid Membrane Is Independent of Its Surface Charge.Biomolecules · 2024Article
- Structural Insights into Plant Viruses Revealed by Small-Angle X-ray Scattering and Atomic Force Microscopy.Viruses · 2024Review
- Influenza A Virus M1 Protein Non-Specifically Deforms Charged Lipid Membranes and Specifically Interacts with the Raft Boundary.Membranes · 2023Article
- pH-dependent endocytosis mechanisms for influenza A and SARS-coronavirus.Frontiers in microbiology · 2023Review
- An overview of influenza A virus genes, protein functions, and replication cycle highlighting important updates.Virus genes · 2022Review
- Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- Recent Progress in Recombinant Influenza Vaccine Development Toward Heterosubtypic Immune Response.Frontiers in immunology · 2022Review
- Article
- Review
- Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design.Computational and structural biotechnology journal · 2020Review
- The dimeric ectodomain of the alkali-sensing insulin receptor-related receptor (ectoIRR) has a droplike shape.The Journal of biological chemistry · 2019Article
- Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization.Bioscience reports · 2019Article
- Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH.Journal of virology · 2019Article
- Model of influenza virus acidification.PloS one · 2019Article
- Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement.Frontiers in immunology · 2018Review
- Pandemic Avian Influenza and Intra/Interhaemagglutinin Subtype Electrostatic Variation among Viruses Isolated from Avian, Mammalian, and Human Hosts.BioMed research international · 2018Article
- Activity-dependent conformational transitions of the insulin receptor-related receptor.The Journal of biological chemistryArticle
- Conformational triggers associated with influenza matrix protein 1 polymerization.The Journal of biological chemistryArticle
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13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus matrix protein M1 plays an essential role in the virus lifecycle, but its functional and structural properties are not entirely defined. Here we employed small-angle X-ray scattering, atomic force microscopy and zeta-potential measurements to characterize the overall structure and association behavior of the full-length M1 at different pH conditions. We demonstrate that the protein consists of a globular N-terminal domain and a flexible C-terminal extension. The globular N-terminal domain of M1 monomers appears preserved in the range of pH from 4.0 to 6.8, while the C-terminal domain remains flexible and the tendency to form multimers changes dramatically. We found that the protein multimerization process is reversible, whereby the binding between M1 molecules starts to break around pH 6. A predicted electrostatic model of M1 self-assembly at different pH revealed a good agreement with zeta-potential measurements, allowing one to assess the role of M1 domains in M1-M1 and M1-lipid interactions. Together with the protein sequence analysis, these results provide insights into the mechanism of M1 scaffold formation and the major role of the flexible and disordered C-terminal domain in this process.
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