ArticleNature structural & molecular biology2011
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM.
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 164 papers.
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Who cites it
164 citing papers in PubMed, 256 citations in OpenAlex.
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- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins.Cell host & microbe · 2026Article
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- Protein-Protein Interactions Analyzed by the Fragment Molecular Orbital Method.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Quantitative evaluation of SLAM receptor-mediated enhancement in canine distemper virus detection: insights from viability, AUC, and MED analyses.In vitro cellular & developmental biology. Animal · 2026Article
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- Evaluation of Measles Vaccine Immunogenicity and Durability Using A Pseudotyped Virus Neutralization Assay.China CDC weekly · 2025Article
- Evolutionary and structural basis of SLAMF1 utilization in morbilliviruses-Implications for host range and cross-species transmission.PLoS pathogens · 2025Article
- Ecology and evolutionary trajectories of morbilliviruses in Neotropical bats.Nature microbiology · 2025Article
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- Genetic analyses and functional validation of ruminant SLAMs reveal potential hosts for PPRV.Veterinary research · 2025Article
- Development of a potent neutralizing nanobody against canine distemper virus hemagglutinin protein.Frontiers in immunology · 2025Article
- Ongoing measles outbreak in Romania: Clinical investigation and molecular epidemiology performed on whole genome sequences.PloS one · 2025Observational
- Zoonotic Paramyxoviruses: Evolution, Ecology, and Public Health Strategies in a Changing World.Viruses · 2024Review
- Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1.Nature communications · 2024Article
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- Detailed analysis of low temperature inactivation of respiratory syncytial virus.Scientific reports · 2024Article
- Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant.Nature communications · 2024Article
104 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Measles virus, a major cause of childhood morbidity and mortality worldwide, predominantly infects immune cells using signaling lymphocyte activation molecule (SLAM) as a cellular receptor. Here we present crystal structures of measles virus hemagglutinin (MV-H), the receptor-binding glycoprotein, in complex with SLAM. The MV-H head domain binds to a β-sheet of the membrane-distal ectodomain of SLAM using the side of its β-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their β-propeller. The structure provides templates for antiviral drug design, an explanation for the effectiveness of the measles virus vaccine, and a model of the homophilic SLAM-SLAM interaction involved in immune modulations. Notably, the crystal structures obtained show two forms of the MV-H-SLAM tetrameric assembly (dimer of dimers), which may have implications for the mechanism of fusion triggering.
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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.