Evaluation of the Glycan-Binding and Esterase Activities of Hemagglutinin-Esterase-Fusion Glycoprotein from Influenza D Virus.
Esterase
Hemagglutinin assay
Hemagglutinin-esterase-fusion (HEF)
Influenza D virus
Receptor binding
Solid-phase assay
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
29
9
2022
pubmed:
30
9
2022
medline:
4
10
2022
Statut:
ppublish
Résumé
Influenza D virus (IDV) is a new member of influenza virus that uses cattle as the primary reservoir and infects multiple agricultural animals. Similar to influenza C virus (ICV), IDV also has seven segments in its genome and has only one major surface glycoprotein, called the hemagglutinin-esterase-fusion (HEF) protein, for receptor-binding, receptor-destroying, and membrane fusion. HEF utilizes 9-O-acetylated sialic acids as its receptor and has both receptor binding and esterase activities, thus is a critical determinant of host tropism. Here, we summarize the methods to evaluate the glycan-binding and esterase activities of HEF in vitro. The glycan-bind property is monitored through glycan microarray, MDCK cell-binding assay, Hemagglutination assay, solid-phase lectin binding assay, and immunofluorescence of tissue sections, and its esterase property is analyzed via esterase enzymatic activity assay.
Identifiants
pubmed: 36175636
doi: 10.1007/978-1-0716-2635-1_15
doi:
Substances chimiques
Glycoproteins
0
Hemagglutinins
0
Lectins
0
Membrane Glycoproteins
0
Sialic Acids
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
187-203Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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