ArticleNature structural & molecular biology2010
Structure of the measles virus hemagglutinin bound to the CD46 receptor.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 134 citations in OpenAlex.
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- Protein-Protein Interactions Analyzed by the Fragment Molecular Orbital Method.Methods in molecular biology (Clifton, N.J.) · 2026Article
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- Immunologic and Genetic Contributors to CD46-Dependent Immune Dysregulation.Journal of clinical immunology · 2023Article
- Biophysical characterization of the cetacean morbillivirus haemagglutinin glycoprotein.Virus research · 2023Article
- Structure of Bovine CD46 Ectodomain.Viruses · 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
- Unveiling the affinity-stability relationship in anti-measles virus antibodies: a computational approach for hotspots prediction.Frontiers in molecular biosciences · 2023Article
- Hemagglutinin protein of Peste des Petits Ruminants virus (PPRV) activates the innate immune response via Toll-like receptor 2 signaling.Virulence · 2021Article
- Computational Analysis Reveals a Critical Point Mutation in theMolecules (Basel, Switzerland) · 2021Article
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- A durable protective immune response to wild-type measles virus infection of macaques is due to viral replication and spread in lymphoid tissues.Science translational medicine · 2020Article
- HSP70 Multi-Functionality in Cancer.Cells · 2020Review
- 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
- 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
- A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- Marine Morbilliviruses: Diversity and Interaction with Signaling Lymphocyte Activation Molecules.Viruses · 2019Review
30 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The highly contagious measles virus infects millions of individuals worldwide, causing serious disease in children of developing countries. Infection is initiated by attachment of the measles virus hemagglutinin (MV-H), a glycoprotein anchored to the virus envelope, to the host cell receptors CD46 or signaling lymphocyte activation molecule (SLAM). Here we report the crystal structure of MV-H in complex with a CD46 protein spanning the two N-terminal domains. A unique groove at the side of the MV-H beta-propeller domain, which is absent in homologous paramyxovirus attachment proteins, engages residues in both CD46 domains. Key contacts involve a protruding loop in the N-terminal CD46 domain that carries two sequential proline residues (PP motif) and penetrates deeply into a hydrophobic socket in MV-H. We identify a similar PP motif in SLAM, defining a common measles virus recognition epitope in the CD46 and SLAM receptor proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.