ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structures of the prefusion form of measles virus fusion protein in complex with inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. 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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Who cites it
51 citing papers in PubMed, 78 citations in OpenAlex.
- Target-Based Antiviral Drug Development Against Human Respiratory Viruses.Pathogens (Basel, Switzerland) · 2026Review
- Identification and structure-activity relationship analysis of minimal fusion inhibitors targeting measles virus F protein.RSC medicinal chemistry · 2026Article
- Identification of cannabichromevarin as a potent stabilizer of the measles virus prefusion F protein: structural insights from long-timescale molecular dynamics.Scientific reports · 2026Article
- Protection against lethal canine distemper virus infection by a dual epitope-targeting synthetic antibody.Nature communications · 2026Article
- Beyond Processing: Furin as a Central Hub in Viral Pathogenesis and Genetic Susceptibility.Biomolecules · 2025Review
- Structural basis of measles virus polymerase inhibition by nonnucleoside inhibitor ERDRP-0519.Nature communications · 2025Article
- Stabilized Full-Length Measles Fusion Protein Elicits Potent Immunity and Protection In Vivo.bioRxiv : the preprint server for biology · 2025Article
- A Short Peptide Inhibitor of Measles Virus Fusion Protein that Exhibits Passive Membrane Permeability.ChemMedChem · 2025Article
- Amino acid changes accumulated in the fusion protein allow neuropathogenic measles viruses to use a broad repertoire of host factors for cell fusion triggering.Journal of virology · 2025Article
- Structure-based design of glycoprotein subunit vaccines for mumps.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A neutralizing antibody prevents postfusion transition of measles virus fusion protein.Science (New York, N.Y.) · 2024Article
- Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein.Nature communications · 2024Article
- An antifouling membrane-fusogenic liposome for effective intracellular delivery in vivo.Nature communications · 2024Article
- Helical peptides with disordered regions for measles viruses provide new generalized insights into fusion inhibitors.iScience · 2024Article
- Epilepsia Partialis Continua as a Sequelae of Measles Infection in Children With Hematolymphoid Malignancies.JCO global oncology · 2024Article
- Suppression of viral RNA polymerase activity is necessary for persistent infection during the transformation of measles virus into SSPE virus.PLoS pathogens · 2023Article
- Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.Journal of virology · 2023Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
- Structure and supramolecular organization of the canine distemper virus attachment glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Collective fusion activity determines neurotropism of an en bloc transmitted enveloped virus.Science advances · 2023Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Measles virus (MeV), a major cause of childhood morbidity and mortality, is highly immunotropic and one of the most contagious pathogens. MeV may establish, albeit rarely, persistent infection in the central nervous system, causing fatal and intractable neurodegenerative diseases such as subacute sclerosing panencephalitis and measles inclusion body encephalitis. Recent studies have suggested that particular substitutions in the MeV fusion (F) protein are involved in the pathogenesis by destabilizing the F protein and endowing it with hyperfusogenicity. Here we show the crystal structures of the prefusion MeV-F alone and in complex with the small compound AS-48 or a fusion inhibitor peptide. Notably, these independently developed inhibitors bind the same hydrophobic pocket located at the region connecting the head and stalk of MeV-F, where a number of substitutions in MeV isolates from neurodegenerative diseases are also localized. Since these inhibitors could suppress membrane fusion mediated by most of the hyperfusogenic MeV-F mutants, the development of more effective inhibitors based on the structures may be warranted to treat MeV-induced neurodegenerative diseases.
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