ArticlePloS one2012
Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Targeted NanoBiT Screening Identifies a Novel Interaction Between SNAPIN and Influenza A Virus M1 Protein.Biology · 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
- pH-dependent endocytosis mechanisms for influenza A and SARS-coronavirus.Frontiers in microbiology · 2023Review
- Protein Folding Interdiction Strategy for Therapeutic Drug Development in Viral Diseases: Ebola VP40 and Influenza A M1.International journal of molecular sciences · 2022Article
- Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization.Bioscience reports · 2019Article
- Conserved methionine 165 of matrix protein contributes to the nuclear import and is essential for influenza A virus replication.Virology journal · 2018Article
- Evolution of Therapeutic Antibodies, Influenza Virus Biology, Influenza, and Influenza Immunotherapy.BioMed research international · 2018Review
- Maintaining pH-dependent conformational flexibility of M1 is critical for efficient influenza A virus replication.Emerging microbes & infections · 2017Article
- Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.Scientific reports · 2017Article
- The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Scientific reports · 2017Article
- Ubiquitin in Influenza Virus Entry and Innate Immunity.Viruses · 2016Review
- Broad Spectrum Anti-Influenza Agents by Inhibiting Self-Association of Matrix Protein 1.Scientific reports · 2016Article
- Article
- pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane Fusion.Journal of virology · 2016Article
- Article
- Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.Cellular microbiology · 2015Article
- Cell penetrable human scFv specific to middle domain of matrix protein-1 protects mice from lethal influenza.Viruses · 2015Article
- Stepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration.Journal of virology · 2014Article
- Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.Biophysical journal · 2014Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe matrix 1 (M1) protein of Influenza A virus plays many critical roles throughout the virus life cycle. The oligomerization of M1 is essential for the formation of the viral matrix layer during the assembly and budding process. METHODOLOGY/PRINCIPAL
findingsIn the present study, we report that M1 can oligomerize in vitro, and that the oligomerization is pH-dependent. The N-terminal domain of M1 alone exists as multiple-order oligomers at pH 7.4, and the C-terminal domain alone forms an exclusively stable dimer. As a result, intact M1 can display different forms of oligomers and dimer is the smallest oligomerization state, at neutral pH. At pH 5.0, oligomers of the N-terminal domain completely dissociate into monomers, while the C-terminal domain remains in dimeric form. As a result, oligomers of intact M1 dissociate into a stable dimer at acidic pH. CONCLUSIONS/SIGNIFICANCE: Oligomerization of M1 involves both the N- and C-terminal domains. The N-terminal domain determines the pH-dependent oligomerization characteristic, and C-terminal domain forms a stable dimer, which contributes to the dimerization of M1. The present study will help to unveil the mechanisms of influenza A virus assembly and uncoating process.
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