ArticleJournal of virology2005
Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 119 citations in OpenAlex.
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025Review
- 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
- Influenza A virus rapidly adapts particle shape to environmental pressures.Nature microbiology · 2025Article
- A physical model for M1-mediated influenza A virus assembly.Biophysical journal · 2025Article
- PSMD12-Mediated M1 Ubiquitination of Influenza A Virus at K102 Regulates Viral Replication.Journal of virology · 2022Article
- Multiple Gene Segments Are Associated with Enhanced Virulence of Clade 2.3.4.4 H5N8 Highly Pathogenic Avian Influenza Virus in Mallards.Journal of virology · 2021Article
- Acetylation, Methylation and Allysine Modification Profile of Viral and Host Proteins during Influenza A Virus Infection.Viruses · 2021Article
- Article
- Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer.PLoS biology · 2020Article
- Dysregulation of M segment gene expression contributes to influenza A virus host restriction.PLoS pathogens · 2019Article
- Super-resolution microscopy reveals significant impact of M2e-specific monoclonal antibodies on influenza A virus filament formation at the host cell surface.Scientific reports · 2019Article
- A Novel Type of Influenza A Virus-Derived Defective Interfering Particle with Nucleotide Substitutions in Its Genome.Journal of virology · 2019Article
- Review
- Article
- Article
- CypA Regulates AIP4-Mediated M1 Ubiquitination of Influenza A Virus.Virologica Sinica · 2018Article
- Structural analysis of influenza vaccine virus-like particles reveals a multicomponent organization.Scientific reports · 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
11 more citing papers are in PubMed but not listed here.
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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Several functions required for the replication of influenza A viruses have been attributed to the viral matrix protein (M1), and a number of studies have focused on a region of the M1 protein designated "helix six." This region contains an exposed positively charged stretch of amino acids, including the motif 101-RKLKR-105, which has been identified as a nuclear localization signal, but several studies suggest that this domain is also involved in functions such as binding to the ribonucleoprotein genome segments (RNPs), membrane association, interaction with the viral nuclear export protein, and virus assembly. In order to define M1 functions in more detail, a series of mutants containing alanine substitutions in the helix six region were generated in A/WSN/33 virus. These were analyzed for RNP-binding function, their capacity to incorporate into infectious viruses by using reverse genetics, the replication properties of rescued viruses, and the morphological phenotypes of the mutant virus particles. The most notable effect that was identified concerned single amino acid substitution mutants that caused significant alterations to the morphology of budded viruses. Whereas A/WSN/33 virus generally forms particles that are predominantly spherical, observations made by negative stain electron microscopy showed that several of the mutant virions, such as K95A, K98A, R101A, and K102A, display a wide range of shapes and sizes that varied in a temperature-dependent manner. The K102A mutant is particularly interesting in that it can form extended filamentous particles. These results support the proposition that the helix six domain is involved in the process of virus assembly.
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Registered trials
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.