Structural basis for Glycan-receptor binding by mumps virus hemagglutinin-neuraminidase.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
31 01 2020
31 01 2020
Historique:
received:
25
10
2019
accepted:
16
01
2020
entrez:
2
2
2020
pubmed:
2
2
2020
medline:
18
11
2020
Statut:
epublish
Résumé
Mumps virus is one of the main cause of respiratory illnesses in humans, especially children. Among the viral surface glycoproteins, the hemagglutinin - neuraminidase, MuV-HN, plays key roles in virus entry into host cells and infectivity, thus representing an ideal target for the design of novel inhibitors. Here we report the detailed analysis of the molecular recognition of host cell surface sialylated glycans by the viral glycoprotein MuV-HN. By a combined use of NMR, docking, molecular modelling and CORCEMA-ST, the structural features of sialoglycans/MuV-HN complexes were revealed. Evidence for a different enzyme activity toward longer and complex substrates compared to unbranched ligands was also examined by an accurate NMR kinetic analysis. Our results provide the basis for the structure-based design of effective drugs against mumps-induced diseases.
Identifiants
pubmed: 32005959
doi: 10.1038/s41598-020-58559-6
pii: 10.1038/s41598-020-58559-6
pmc: PMC6994497
doi:
Substances chimiques
Hemagglutinins
0
Polysaccharides
0
Viral Structural Proteins
0
Neuraminidase
EC 3.2.1.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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