ArticleProceedings of the National Academy of Sciences of the United States of America2016
Trisaccharide containing α2,3-linked sialic acid is a receptor for mumps virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.
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Who cites it
69 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Anti-cancer efficacy of combined vaccine-strain measles and mumps viruses against colorectal cancer: an experimental study.Molecular biology reports · 2026Article
- Lineage Diversification and Evolutionary Dynamics of theMicroorganisms · 2026Article
- Defining the molecular interaction between influenza hemagglutinin and MHC-II.bioRxiv : the preprint server for biology · 2026Article
- Molecular basis for occlusion of the jeilongvirus receptor-binding site by the elongated C-terminus.mBio · 2026Article
- Mumps Virus: Replication, Immune Response, and the Changing Landscape of Vaccine Effectiveness.Pathogens (Basel, Switzerland) · 2026Review
- Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening.Emerging microbes & infections · 2025Article
- Development of mumps virus-specific sialidase imaging probes through chemical modifications of sialic acid.Scientific reports · 2025Article
- Enhanced visualization of influenza A virus entry into living cells using virus-view atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Sialic acid serves as a functional receptor for grass carp reovirus.PLoS pathogens · 2025Article
- A pan-respiratory virus attachment inhibitor with high potency in human airway models and in vivo.Science advances · 2025Article
- A Comprehensive Bibliometric Analysis of Orchitis Research from 1980 to 2023.Advances in experimental medicine and biology · 2025Review
- SLC35A2 gene product modulates paramyxovirus fusion events during infection.PLoS pathogens · 2025Article
- Structure-based design of glycoprotein subunit vaccines for mumps.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Deep mutational scanning of H5 hemagglutinin to inform influenza virus surveillance.PLoS biology · 2024Article
- Zoonotic Paramyxoviruses: Evolution, Ecology, and Public Health Strategies in a Changing World.Viruses · 2024Review
- Article
- Unraveling dynamics of paramyxovirus-receptor interactions using nanoparticles displaying hemagglutinin-neuraminidase.PLoS pathogens · 2024Article
- Molecular characterization of Mumps virus genotype C detected from Dibrugarh district of Assam, India.The Indian journal of medical research · 2024Article
- Review
9 more citing papers are in PubMed but not listed here.
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Authors and funding
16 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mumps virus (MuV) remains an important pathogen worldwide, causing epidemic parotitis, orchitis, meningitis, and encephalitis. Here we show that MuV preferentially uses a trisaccharide containing α2,3-linked sialic acid in unbranched sugar chains as a receptor. Crystal structures of the MuV attachment protein hemagglutinin-neuraminidase (MuV-HN) alone and in complex with the α2,3-sialylated trisaccharide revealed that in addition to the interaction between the MuV-HN active site residues and sialic acid, other residues, including an aromatic residue, stabilize the third sugar of the trisaccharide. The importance of the aromatic residue and the third sugar in the MuV-HN-receptor interaction was confirmed by computational energy calculations, isothermal titration calorimetry studies, and glycan-binding assays. Furthermore, MuV-HN was found to bind more efficiently to unbranched α2,3-sialylated sugar chains compared with branched ones. Importantly, the strategically located aromatic residue is conserved among the HN proteins of sialic acid-using paramyxoviruses, and alanine substitution compromised their ability to support cell-cell fusion. These results suggest that not only the terminal sialic acid but also the adjacent sugar moiety contribute to receptor function for mumps and these paramyxoviruses. The distribution of structurally different sialylated glycans in tissues and organs may explain in part MuV's distinct tropism to glandular tissues and the central nervous system. In the crystal structure, the epitopes for neutralizing antibodies are located around the α-helices of MuV-HN that are not well conserved in amino acid sequences among different genotypes of MuV. This may explain the fact that MuV reinfection sometimes occurs.
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