N-Linked Glycosylation in the Hemagglutinin of Influenza A Viruses

Research output: Contribution to journalReview article

31 Citations (Scopus)

Abstract

Since the 1918 influenza A virus (IAV) pandemic, H1N1 viruses have circulated in human populations. The hemagglutinin (HA) of IAV determines viral antigenicity and often undergoes N-linked glycosylation (NLG) at several sites. Interestingly, structural analysis of the 1918 and 2009 H1N1 pandemic viruses revealed antigenic similarities attributable to the conserved epitopes and the NLG statuses of their HA proteins. NLG of the globular head of HA is known to modulate the antigenicity, fusion activity, virulence, receptor-binding specificity, and immune evasion of IAV. In addition, the HA of IAV often retains additional mutations. These supplemental mutations compensate for the attenuation of viral properties resulting from the introduced NLG. In human H1N1 viruses, the number and location of NLG sites has been regulated in accordance with the antigenic variability of the NLG-targeted antibody-binding site. The relationship between the NLG and the antigenic variance in HA appears to be stably controlled in the viral context.

Original languageEnglish
Pages (from-to)886-893
Number of pages8
JournalYonsei Medical Journal
Volume53
Issue number5
DOIs
Publication statusPublished - 2012 Jul 1
Externally publishedYes

Fingerprint

Influenza A virus
Hemagglutinins
Glycosylation
H1N1 Subtype Influenza A Virus
Pandemics
Antibody Binding Sites
Immune Evasion
Antigenic Variation
Mutation
Virulence
Epitopes
Population
Proteins

Keywords

  • Glycosylation
  • Hemagglutinin
  • Influenza virus
  • Pandemic

ASJC Scopus subject areas

  • Medicine(all)

Cite this

N-Linked Glycosylation in the Hemagglutinin of Influenza A Viruses. / Kim, Jin Il; Park, Man-Seong.

In: Yonsei Medical Journal, Vol. 53, No. 5, 01.07.2012, p. 886-893.

Research output: Contribution to journalReview article

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