ArticlePLoS biology2020
Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer.
Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 35 citations in OpenAlex.
- Covalently Immobilized Lignin-Xanthene Conjugates for Persistent Surface Photochemistry and Self-Sterilizing Interfaces Under Ambient Visible Light.Macromolecular rapid communications · 2026Article
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- A novel accessory gene product of tick-borne Dhori-Orthomyxovirus, encoded by overlooked spliced transcripts of RNA segment 6.Journal of virology · 2025Article
- Visualizing influenza A virus assembly by in situ cryo-electron tomography.Nature communications · 2025Article
- TfR1 facilitates influenza virus endocytosis and uncoating by interacting with NA and M1 via extracellular and intracellular domains.PLoS pathogens · 2025Article
- Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025Review
- Bisbenzylisoquinoline alkaloids inhibit influenza virus replication by disrupting endosomal acidification.Virology journal · 2025Article
- Visualizing and analyzing 3D biomolecular structures using Mol* at RCSB.org: Influenza A H5N1 virus proteome case study.Protein science : a publication of the Protein Society · 2025Article
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- A physical model for M1-mediated influenza A virus assembly.Biophysical journal · 2025Article
- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
- Region-selective and site-specific glycation of influenza proteins surrounding the viral envelope membrane.Scientific reports · 2024Article
- A Fluorogenic Pseudoinfection Assay to Probe Transfer and Distribution of Influenza Viral Contents to Target Vesicles.Analytical chemistry · 2024Article
- Review
- Peptide Models of the Cytoplasmic Tail of Influenza A/H1N1 Virus Hemagglutinin Expand Understanding its pH-Dependent Modes of Interaction with Matrix Protein M1.The protein journal · 2023Article
- Polydopamine-based nanomedicines for efficient antiviral and secondary injury protection therapy.Science advances · 2023Article
- TRIM21 restricts influenza A virus replication by ubiquitination-dependent degradation of M1.PLoS pathogens · 2023Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Matrix proteins are encoded by many enveloped viruses, including influenza viruses, herpes viruses, and coronaviruses. Underneath the viral envelope of influenza virus, matrix protein 1 (M1) forms an oligomeric layer critical for particle stability and pH-dependent RNA genome release. However, high-resolution structures of full-length monomeric M1 and the matrix layer have not been available, impeding antiviral targeting and understanding of the pH-dependent transitions involved in cell entry. Here, purification and extensive mutagenesis revealed protein-protein interfaces required for the formation of multilayered helical M1 oligomers similar to those observed in virions exposed to the low pH of cell entry. However, single-layered helical oligomers with biochemical and ultrastructural similarity to those found in infectious virions before cell entry were observed upon mutation of a single amino acid. The highly ordered structure of the single-layered oligomers and their likeness to the matrix layer of intact virions prompted structural analysis by cryo-electron microscopy (cryo-EM). The resulting 3.4-Å-resolution structure revealed the molecular details of M1 folding and its organization within the single-shelled matrix. The solution of the full-length M1 structure, the identification of critical assembly interfaces, and the development of M1 assembly assays with purified proteins are crucial advances for antiviral targeting of influenza viruses.
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