The role of glycosylation in the N-terminus of the hemagglutinin of a unique H4N2 with a natural polybasic cleavage site in virus fitness
Highly pathogenic
avian influenza virus
glycosylation
h4n2
hemagglutinin
low pathogenic
non-H5/H7
proteolytic activation
transmission
virulence
Journal
Virulence
ISSN: 2150-5608
Titre abrégé: Virulence
Pays: United States
ID NLM: 101531386
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
entrez:
4
2
2021
pubmed:
5
2
2021
medline:
1
10
2021
Statut:
ppublish
Résumé
To date, only low pathogenic (LP) H5 and H7 avian influenza viruses (AIV) have been observed to naturally shift to a highly pathogenic (HP) phenotype after mutation of the monobasic hemagglutinin (HA) cleavage site (HACS) to polybasic motifs. The LPAIV monobasic HACS is activated by tissue-restricted trypsin-like enzymes, while the HPAIV polybasic HACS is activated by ubiquitous furin-like enzymes. However, glycosylation near the HACS can affect proteolytic activation and reduced virulence of some HPAIV in chickens. In 2012, a unique H4N2 virus with a polybasic HACS was isolated from quails but was LP in chickens. Whether glycosylation sites (GS) near the HACS hinder the evolution of HPAIV H4N2 remains unclear. Here, we analyzed the prevalence of potential GS in the N-terminus of HA1,
Identifiants
pubmed: 33538209
doi: 10.1080/21505594.2021.1881344
pmc: PMC7872060
doi:
Substances chimiques
Hemagglutinins, Viral
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
666-678Références
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