ArticleProceedings of the National Academy of Sciences of the United States of America2014
Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 77 citations in OpenAlex.
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- ZFP91 restricts RSV replication by driving K48-linked ubiquitination and proteasomal degradation of M2-1.Cellular and molecular life sciences : CMLS · 2026Article
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.Science advances · 2026Article
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- Epidemiological characteristics and whole-genome analysis of respiratory syncytial virus in Jining city from February 2023 to December 2024.Frontiers in microbiology · 2026Article
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- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Expression and Purification of Recombinant Respiratory Syncytial Virus Proteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Single-Particle Electron Microscopy Analysis of Respiratory Syncytial Virus Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Biophysical Characterization of the MMethods in molecular biology (Clifton, N.J.) · 2025Article
- 8-Oxoguanine DNA Glycosylase1 conceals oxidized guanine in nucleoprotein-associated RNA of respiratory syncytial virus.PLoS pathogens · 2024Article
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- Hardening of Respiratory Syncytial Virus Inclusion Bodies by Cyclopamine Proceeds through Perturbation of the Interactions of the M2-1 Protein with RNA and the P Protein.International journal of molecular sciences · 2023Article
- Assembly of the Tripartite and RNA Condensates of the Respiratory Syncytial Virus Factory ProteinsViruses · 2023Article
- Helical ordering of envelope-associated proteins and glycoproteins in respiratory syncytial virus.The EMBO journal · 2022Article
- Review
- Respiratory syncytial virus M2-1 protein associates non-specifically with viral messenger RNA and with specific cellular messenger RNA transcripts.PLoS pathogens · 2021Article
- Pneumoviral Phosphoprotein, a Multidomain Adaptor-Like Protein of Apparent Low Structural Complexity and High Conformational Versatility.International journal of molecular sciences · 2021Review
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
The M2-1 protein of the important pathogen human respiratory syncytial virus is a zinc-binding transcription antiterminator that is essential for viral gene expression. We present the crystal structure of full-length M2-1 protein in its native tetrameric form at a resolution of 2.5 Å. The structure reveals that M2-1 forms a disk-like assembly with tetramerization driven by a long helix forming a four-helix bundle at its center, further stabilized by contact between the zinc-binding domain and adjacent protomers. The tetramerization helix is linked to a core domain responsible for RNA binding activity by a flexible region on which lie two functionally critical serine residues that are phosphorylated during infection. The crystal structure of a phosphomimetic M2-1 variant revealed altered charge density surrounding this flexible region although its position was unaffected. Structure-guided mutagenesis identified residues that contributed to RNA binding and antitermination activity, revealing a strong correlation between these two activities, and further defining the role of phosphorylation in M2-1 antitermination activity. The data we present here identify surfaces critical for M2-1 function that may be targeted by antiviral compounds.
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