ArticleThe Journal of biological chemistry2008
Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150).
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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Who cites it
45 citing papers in PubMed, 75 citations in OpenAlex.
- Protein-Protein Interactions Analyzed by the Fragment Molecular Orbital Method.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Genetic analyses and functional validation of ruminant SLAMs reveal potential hosts for PPRV.Veterinary research · 2025Article
- Structure, Attachment and Transmembrane Internalisation of Peste Des Petits Ruminants Virus.Veterinary medicine and science · 2025Review
- Cell-Int: a cell-cell interaction assay to identify native membrane protein interactions.Life science alliance · 2024Article
- Quantitative assays reveal cell fusion at minimal levels of SARS-CoV-2 spike protein and fusion from without.iScience · 2021Article
- MeV-Stealth: A CD46-specific oncolytic measles virus resistant to neutralization by measles-immune human serum.PLoS pathogens · 2021Article
- Measles Virus as an Oncolytic Immunotherapy.Cancers · 2021Review
- Engineering and combining oncolytic measles virus for cancer therapy.Cytokine & growth factor reviews · 2020Review
- Identification of correlated inter-residue interactions in protein complex based on the fragment molecular orbital method.Journal of molecular graphics & modelling · 2020Article
- 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
- Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.The Journal of biological chemistry · 2020Review
- Expanding Diversity of Susceptible Hosts in Peste Des Petits Ruminants Virus Infection and Its Potential Mechanism Beyond.Frontiers in veterinary science · 2020Review
- Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- Regulatory Role of the Morbillivirus Attachment Protein Head-to-Stalk Linker Module in Membrane Fusion Triggering.Journal of virology · 2018Article
- Canine Distemper Virus Spread and Transmission to Naive Ferrets: Selective Pressure on Signaling Lymphocyte Activation Molecule-Dependent Entry.Journal of virology · 2018Article
- Measles Vaccine.Viral immunology · 2018Review
- Hemagglutinin-specific neutralization of subacute sclerosing panencephalitis viruses.PloS one · 2018Article
- The Host Cell Receptors for Measles Virus and Their Interaction with the Viral Hemagglutinin (H) Protein.Viruses · 2016Review
- 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
9 authors at 4 institutions in 3 countries.
Funding
Abstract
The interaction of measles virus with its receptor signaling lymphocytic activation molecule (SLAM) controls cell entry and governs tropism. We predicted potential interface areas of the measles virus attachment protein hemagglutinin to begin the investigation. We then assessed the relevance of individual amino acids located in these areas for SLAM-binding and SLAM-dependent membrane fusion, as measured by surface plasmon resonance and receptor-specific fusion assays, respectively. These studies identified one hemagglutinin protein residue, isoleucine 194, which is essential for primary binding. The crystal structure of the hemagglutinin-protein localizes Ile-194 at the interface of propeller blades 5 and 6, and our data indicate that a small aliphatic side chain of residue 194 stabilizes a protein conformation conducive to binding. In contrast, a quartet of residues previously shown to sustain SLAM-dependent fusion is not involved in binding. Instead, our data prove that after binding, this quartet of residues on propeller blade 5 conducts conformational changes that are receptor-specific. Our study sets a structure-based stage for understanding how the SLAM-elicited conformational changes travel through the H-protein ectodomain before triggering fusion protein unfolding and membrane fusion.
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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.