ArticleThe Journal of biological chemistry2012
Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 39 citations in OpenAlex.
- Structural and mechanistic basis for antibody neutralization of the measles fusion protein.Nature communications · 2026Article
- The measles virus matrix F50S mutation from a lethal case of subacute sclerosing panencephalitis promotes receptor-independent neuronal spread.Journal of virology · 2025Article
- Structural basis for potent neutralization of human respirovirus type 3 by protective single-domain camelid antibodies.Nature communications · 2024Article
- A Quantitative Fusion Assay to Study Measles Virus Entry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.The Journal of biological chemistry · 2020Review
- A comprehensive global perspective on phylogenomics and evolutionary dynamics of Small ruminant morbillivirus.Scientific reports · 2020Article
- 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
- Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.Nature communications · 2017Article
- Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.Journal of virology · 2016Article
- Mutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.Journal of virology · 2016Article
- Review
- Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- LaSota fusion (F) cleavage motif-mediated fusion activity is affected by other regions of the F protein from different genotype Newcastle disease virus in a chimeric virus: implication for virulence attenuation.The Journal of general virology · 2016Article
- Review
- Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A Structurally Unresolved Head Segment of Defined Length Favors Proper Measles Virus Hemagglutinin Tetramerization and Efficient Membrane Fusion Triggering.Journal of virology · 2016Article
- Review
- Measles virus glycoprotein complexes preassemble intracellularly and relax during transport to the cell surface in preparation for fusion.Journal of virology · 2015Article
- Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Journal of virology · 2015Article
- Mutations in the DI-DII Linker of Human Parainfluenza Virus Type 3 Fusion Protein Result in Diminished Fusion Activity.PloS one · 2015Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The measles virus (MV) fusion (F) protein trimer executes membrane fusion after receiving a signal elicited by receptor binding to the hemagglutinin (H) tetramer. Where and how this signal is received is understood neither for MV nor for other paramyxoviruses. Because only the prefusion structure of the parainfluenza virus 5 (PIV5) F-trimer is available, to study signal receipt by the MV F-trimer, we generated and energy-refined a homology model. We used two approaches to predict surface residues of the model interacting with other proteins. Both approaches measured interface propensity values for patches of residues. The second approach identified, in addition, individual residues based on the conservation of physical chemical properties among F-proteins. Altogether, about 50 candidate interactive residues were identified. Through iterative cycles of mutagenesis and functional analysis, we characterized six residues that are required specifically for signal transmission; their mutation interferes with fusion, although still allowing efficient F-protein processing and cell surface transport. One residue is located adjacent to the fusion peptide, four line a cavity in the base of the F-trimer head, while the sixth residue is located near this cavity. Hydrophobic interactions in the cavity sustain the fusion process and contacts with H. The cavity is flanked by two different subunits of the F-trimer. Tetrameric H-stalks may be lodged in apposed cavities of two F-trimers. Because these insights are based on a PIV5 homology model, the signal receipt mechanism may be conserved among paramyxoviruses.
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