N-Linked Glycosylation in the Hemagglutinin of Influenza A Viruses.
10.3349/ymj.2012.53.5.886
- Author:
Jin Il KIM
1
;
Man Seong PARK
Author Information
1. Department of Microbiology, Center for Medical Science Research, College of Medicine, Hallym University, Chuncheon, Korea. ms0392@hallym.ac.kr
- Publication Type:Review ; Research Support, Non-U.S. Gov't
- Keywords:
Glycosylation;
hemagglutinin;
influenza virus;
pandemic
- MeSH:
Antigenic Variation;
Epitopes;
Glycosylation*;
Head;
Hemagglutinins*;
Humans;
Immune Evasion;
Influenza A virus*;
Influenza A Virus, H1N1 Subtype;
Influenza, Human*;
Orthomyxoviridae;
Pandemics;
Sensitivity and Specificity;
Virulence
- From:Yonsei Medical Journal
2012;53(5):886-893
- CountryRepublic of Korea
- Language:English
-
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.
