ReviewViruses2016
Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability.
Review in Viruses, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- Distinct Humoral Response Development to Measles Virus Across Vaccine Platforms.The Journal of infectious diseases · 2026Article
- Reconstructing pathogen-specific antibody binding epitopes and age-dependent immune signatures from proteomic-scale peptide libraries.Science advances · 2026Article
- From sites to structure to serology: a roadmap for structure-aware molecular evolution of antigenically evolving viruses.Journal of virology · 2026Review
- Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins.Cell host & microbe · 2026Article
- Measles challenges: global resurgence and factors affecting eradication.Italian journal of pediatrics · 2026Review
- Localized adaptive evolution in VP1 drives antigenic divergence of feline calicivirus despite high sequence conservation.Veterinary research · 2026Article
- Reconstructing pathogen-specific antibody binding epitopes and age-dependent immune signatures from proteomic-scale peptide libraries.medRxiv : the preprint server for health sciences · 2025Article
- Construction and Preclinical Evaluation of a Recombinant Attenuated Measles Vaccine Candidate of the H1a Genotype.Vaccines · 2025Article
- Advances in Surrogate Neutralization Tests for High-Throughput Screening and the Point-of-Care.Analytical chemistry · 2025Review
- Glycosylation as a strategic mechanism for measles virus and mumps virus immune evasion.Frontiers in immunology · 2025Review
- Ongoing measles outbreak in Romania: Clinical investigation and molecular epidemiology performed on whole genome sequences.PloS one · 2025Observational
- Neutralizing Antibody Response to Genotypically Diverse Measles Viruses in Clinically Suspected Measles Cases.Viruses · 2023Article
- 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
- Article
- Development of a Measles and Rubella Multiplex Bead Serological Assay for Assessing Population Immunity.Journal of clinical microbiology · 2021Article
- Serotypic evolution of measles virus is constrained by multiple co-dominant B cell epitopes on its surface glycoproteins.Cell reports. Medicine · 2021Article
- Molecular Epidemiology of B3 and D8 Measles Viruses through Hemagglutinin Phylogenetic History.International journal of molecular sciences · 2020Article
- Article
- Article
- Structure-Guided Identification of a Nonhuman Morbillivirus with Zoonotic Potential.Journal of virology · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Globally eliminating measles using available vaccines is biologically feasible because the measles virus (MV) hemagglutinin (H) protein is antigenically stable. The H protein is responsible for receptor binding, and is the main target of neutralizing antibodies. The immunodominant epitope, known as the hemagglutinating and noose epitope, is located near the receptor-binding site (RBS). The RBS also contains an immunodominant epitope. Loss of receptor binding correlates with an escape from the neutralization by antibodies that target the epitope at RBS. Another neutralizing epitope is located near RBS and is shielded by an N-linked sugar in certain genotype strains. However, human sera from vaccinees and measles patients neutralized all MV strains with similar efficiencies, regardless of the N-linked sugar modification or mutations at these epitopes. Two other major epitopes exist at a distance from RBS. One has an unstructured flexible domain with a linear neutralizing epitope. When MV-H forms a tetramer (dimer of dimers), these epitopes may form the dimer-dimer interface, and one of the two epitopes may also interact with the F protein. The neutralization mechanisms of antibodies that recognize these epitopes may involve inhibiting the H-F interaction or blocking the fusion cascade after MV-H binds to its receptors.
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What OpenQuestion holds
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.