ArticleCellular microbiology2015
Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.
Article in Cellular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- Inhibitory effects of a hot-water extract of cumin fruit on influenza A virus infection.PloS one · 2025Article
- Region-selective and site-specific glycation of influenza proteins surrounding the viral envelope membrane.Scientific reports · 2024Article
- Adaptation potential of H3N8 canine influenza virus in human respiratory cells.Scientific reports · 2024Article
- Structural dynamics of SARS-CoV-2 nucleocapsid protein induced by RNA binding.PLoS computational biology · 2022Article
- Article
- Conserved methionine 165 of matrix protein contributes to the nuclear import and is essential for influenza A virus replication.Virology journal · 2018Article
- Genetic Analysis of the M Gene of Equine Influenza Virus Strains Isolated in Poland, in the Context of the Asian-like Group Formation.Journal of veterinary research · 2018Article
- Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.Journal of virology · 2018Article
- Maintaining pH-dependent conformational flexibility of M1 is critical for efficient influenza A virus replication.Emerging microbes & infections · 2017Article
- The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Scientific reports · 2017Article
- Conformational triggers associated with influenza matrix protein 1 polymerization.The Journal of biological chemistryArticle
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9 authors.
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Abstract
The matrix protein 1 (M1) is the most abundant structural protein in influenza A virus particles. It oligomerizes to form the matrix layer under the lipid membrane, sustaining stabilization of the morphology of the virion. The present study indicates that M1 forms oligomers based on a fourfold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of M1 was controlled by a highly conserved region within the C-terminal domain. Two polar residues of this region, serine-183 (S183) and threonine-185 (T185), were identified to be critical for the oligomerization pattern of M1. M1 point mutants suggest that single S183A or T185A substitution could result in the production of morphologically filamentous particles, while double substitutions, M1-S183A/T185A, totally disrupted the fourfold symmetry and resulted in the failure of virus production. These data indicate that the polar groups in these residues are essential to control the oligomerization pattern of M1. Thus, the present study will aid in determining the mechanisms of influenza A virus matrix layer formation during virus morphogenesis.
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