ArticleNature structural & molecular biology2011
The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed.
- Article
- Forskolin Enhances Antitumor Effect of Oncolytic Measles Virus by Promoting Rab27a Dependent Vesicular Transport System.Current microbiology · 2024Article
- A Quantitative Fusion Assay to Study Measles Virus Entry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
- Screening of candidate genes associated with high titer production of oncolytic measles virus based on systems biology approach.Virus genes · 2022Article
- Short-Stalk Isoforms of CADM1 and CADM2 Trigger Neuropathogenic Measles Virus-Mediated Membrane Fusion by Interacting with the Viral Hemagglutinin.Journal of virology · 2022Article
- EphrinB2 clustering by Nipah virus G is required to activate and trap F intermediates at supported lipid bilayer-cell interfaces.Science advances · 2021Article
- Human parainfluenza virus fusion complex glycoproteins imaged in action on authentic viral surfaces.PLoS pathogens · 2020Article
- Type 1 Interferon Responses Underlie Tumor-Selective Replication of Oncolytic Measles Virus.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.The Journal of biological chemistry · 2020Review
- Disruption of the Dimer-Dimer Interaction of the Mumps Virus Attachment Protein Head Domain, Aided by an Anion Located at the Interface, Compromises Membrane Fusion Triggering.Journal of virology · 2020Article
- Roles of the highly conserved amino acids in the second receptor binding site of the Newcastle disease virus HN protein.Virology journal · 2019Article
- Conformational changes in Chikungunya virus E2 protein upon heparan sulfate receptor binding explain mechanism of E2-E1 dissociation during viral entry.Bioscience reports · 2019Article
- A key anti-viral protein, RSAD2/VIPERIN, restricts the release of measles virus from infected cells.Virus research · 2019Article
- Regulatory Role of the Morbillivirus Attachment Protein Head-to-Stalk Linker Module in Membrane Fusion Triggering.Journal of virology · 2018Article
- Functional analysis of amino acids at stalk/head interface of human parainfluenza virus type 3 hemagglutinin-neuraminidase protein in the membrane fusion process.Virus genes · 2018Article
- Measles virus: Background and oncolytic virotherapy.Biochemistry and biophysics reports · 2018Review
- Clinical Trials with Oncolytic Measles Virus: Current Status and Future Prospects.Current cancer drug targets · 2018Review
- Mutations in the Fusion Protein of Measles Virus That Confer Resistance to the Membrane Fusion Inhibitors Carbobenzoxy-d-Phe-l-Phe-Gly and 4-Nitro-2-Phenylacetyl Amino-Benzamide.Journal of virology · 2017Article
- Measles Virus Enters Breast and Colon Cancer Cell Lines through a PVRL4-Mediated Macropinocytosis Pathway.Journal of virology · 2017Article
16 more citing papers are in PubMed but not listed here.
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Funding
Abstract
The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.
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