Measuring Site-specific Glycosylation Similarity between Influenza a Virus Variants with Statistical Certainty.

ABSTRACT: Influenza A virus (IAV) mutates rapidly, resulting in antigenic drift and poor year-to-year vaccine effectiveness. One challenge in designing effective vaccines is that genetic mutations frequently cause amino acid variations in IAV envelope protein hemagglutinin (HA) that create new N-glycosylation sequons; resulting N-glycans cause antigenic shielding, allowing viral escape from adaptive immune responses. Vaccine candidate strain selection currently involves correlating antigenicity with HA protein sequence among circulating strains, but quantitative comparison of site-specific glycosylation information may likely improve the ability to design vaccines with broader effectiveness against evolving strains. However, there is poor understanding of the influence of glycosylation

SUBMITTER: Chang D 

PROVIDER: S-EPMC8143645 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature