ArticleJournal of virology2007
Multiple amino acid substitutions in hemagglutinin are necessary for wild-type measles virus to acquire the ability to use receptor CD46 efficiently.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 70 citations in OpenAlex.
- Broad permissiveness of mammalian nectin-4 orthologs for morbilliviruses: a notable exception in dolphin nectin-4.The Journal of general virology · 2026Article
- Evolutionary and structural basis of SLAMF1 utilization in morbilliviruses-Implications for host range and cross-species transmission.PLoS pathogens · 2025Article
- Genetic Characterization of the H Gene of MeV Strains (H1, B3, and D4) Recently Circulated in Iran for Improving the Molecular Measles Surveillance in the National Measles Lab.Iranian journal of public health · 2023Article
- Versatility of live-attenuated measles viruses as platform technology for recombinant vaccines.NPJ vaccines · 2022Review
- Screening of candidate genes associated with high titer production of oncolytic measles virus based on systems biology approach.Virus genes · 2022Article
- Multiple Receptors Involved in Invasion and Neuropathogenicity of Canine Distemper Virus: A Review.Viruses · 2022Review
- A defined anthocyanin mixture sourced from bilberry and black currant inhibits Measles virus and various herpesviruses.BMC complementary medicine and therapies · 2022Article
- Advances in RNA Viral Vector Technology to Reprogram Somatic Cells: The Paramyxovirus Wave.Molecular diagnosis & therapy · 2022Review
- CADM1 and CADM2 Trigger Neuropathogenic Measles Virus-Mediated Membrane Fusion by Acting inJournal of virology · 2021Article
- Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.mSphere · 2021Article
- Measles Virus as an Oncolytic Immunotherapy.Cancers · 2021Review
- Lysosome-Associated Membrane Proteins Support the Furin-Mediated Processing of the Mumps Virus Fusion Protein.Journal of virology · 2020Article
- Non-transmissible MV Vector with Segmented RNA Genome Establishes Different Types of iPSCs from Hematopoietic Cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- WeakJournal of virology · 2020Article
- Measles Virus Hemagglutinin Protein Establishes a Specific Interaction With the Extreme N-Terminal Region of Human Signaling Lymphocytic Activation Molecule to Enhance Infection.Frontiers in microbiology · 2020Article
- Cell-to-Cell Measles Virus Spread between Human Neurons Is Dependent on Hemagglutinin and Hyperfusogenic Fusion Protein.Journal of virology · 2018Article
- Measles Vaccine.Viral immunology · 2018Review
- Measles virus envelope pseudotyped lentiviral vectors transduce quiescent human HSCs at an efficiency without precedent.Blood advances · 2017Article
- Analysis of VSV pseudotype virus infection mediated by rubella virus envelope proteins.Scientific reports · 2017Article
- Dimerization Efficiency of Canine Distemper Virus Matrix Protein Regulates Membrane-Budding Activity.Journal of virology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Measles virus (MV) possesses two envelope glycoproteins, namely, the receptor-binding hemagglutinin (H) and fusion proteins. Wild-type MV strains isolated in B-lymphoid cell lines use signaling lymphocyte activation molecule (SLAM), but not CD46, as a cellular receptor, whereas MV vaccine strains of the Edmonston lineage use both SLAM and CD46 as receptors. Studies have shown that the residue at position 481 of the H protein is critical in determining the use of CD46 as a receptor. However, the wild-type IC-B strain with a single N481Y substitution in the H protein utilizes CD46 rather inefficiently. In this study, a number of chimeric and mutant H proteins, and recombinant viruses harboring them, were generated to determine which residues of the Edmonston H protein are responsible for its efficient use of CD46. Our results show that three substitutions (N390I and E492G plus N416D or T446S), in addition to N481Y, are necessary for the IC-B H protein to use CD46 efficiently as a receptor. The N390I, N416D, and T446S substitutions are present in the H proteins of all strains of the Edmonston lineage, whereas the E492G substitution is found only in the H protein of the Edmonston tag strain generated from cDNAs. The T484N substitution, found in some of the Edmonston-lineage strains, resulted in a similar effect on the use of CD46 to that caused by the E492G substitution. Thus, multiple residues in the H protein that have not previously been implicated have important roles in the interaction with CD46.
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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.