ArticleThe Journal of biological chemistry2012
Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.
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 42 papers.
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Who cites it
42 citing papers in PubMed, 50 citations in OpenAlex.
- Protection against lethal canine distemper virus infection by a dual epitope-targeting synthetic antibody.Nature communications · 2026Article
- A Quantitative Fusion Assay to Study Measles Virus Entry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Clinical Manifestation and Phylogenetic Analysis of Peste des Petits Ruminants in Local Iraqi Breed Sheep in Al-Diwaniyah Province.Veterinary medicine international · 2024Article
- Article
- 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
- Short-Stalk Isoforms of CADM1 and CADM2 Trigger Neuropathogenic Measles Virus-Mediated Membrane Fusion by Interacting with the Viral Hemagglutinin.Journal of virology · 2022Article
- Clustered Lysine Residues of the Canine Distemper Virus Matrix Protein Regulate Membrane Association and Budding Activity.Journal of virology · 2020Article
- Human parainfluenza virus fusion complex glycoproteins imaged in action on authentic viral surfaces.PLoS pathogens · 2020Article
- Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.The Journal of biological chemistry · 2020Review
- Differential Features of Fusion Activation within theViruses · 2020Review
- Regulatory Role of the Morbillivirus Attachment Protein Head-to-Stalk Linker Module in Membrane Fusion Triggering.Journal of virology · 2018Article
- 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
- Measles Virus Enters Breast and Colon Cancer Cell Lines through a PVRL4-Mediated Macropinocytosis Pathway.Journal of virology · 2017Article
- Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.Journal of virology · 2016Article
- The Host Cell Receptors for Measles Virus and Their Interaction with the Viral Hemagglutinin (H) Protein.Viruses · 2016Review
- Paramyxovirus Glycoproteins and the Membrane Fusion Process.Current clinical microbiology reports · 2016Article
- Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly.The Journal of general virology · 2016Article
- Review
- Canine Distemper Virus Fusion Activation: Critical Role of Residue E123 of CD150/SLAM.Journal of virology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The measles virus (MV) fusion apparatus consists of a fusion protein and an attachment protein named hemagglutinin (H). After receptor-binding through its cuboidal head, the H-protein transmits the fusion-triggering signal through its stalk to the fusion protein. However, the structural basis of signal transmission is unclear because only structures of H-heads without their stalk have been solved. On the other hand, the entire ectodomain structure of the hemagglutinin-neuraminidase protein of another Paramyxovirus revealed a four-helix bundle stalk. To probe the structure of the 95-residue MV H-stalk we individually substituted head-proximal residues (positions 103-153) with cysteine, and biochemically and functionally characterized the resultant proteins. Our results indicate that most residues in the central segment (positions 103-117) can be cross-linked by engineered disulfide bonds, and thus may be engaged in a tetrameric structure. While covalent tetramerization disrupts fusion triggering function, disulfide bond reduction restores it in most positions except Asp-113. The next stalk segment (residues 123-138) also has high propensity to form covalent tetramers, but since these cross-links have little or no effect on function, it can conduct the fusion-triggering signal while remaining in a stabilized tetrameric configuration. This segment may act as a spacer, maintaining H-heads at an optimal height. Finally, the head-proximal segment (residues 139-154) has very limited propensity to trap tetramers, suggesting bifurcation into two flexible linkers clamped by inter-subunit covalent links formed by natural Cys-139 and Cys-154. We discuss the modular structure of the MV H-stalk in the context of membrane fusion triggering and cell entry by Paramyxoviruses.
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Registered trials
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