Site-specific glycosylation profile of influenza A (H1N1) hemagglutinin through tandem mass spectrometry.

ABSTRACT: The study of influenza virus evolution in humans has revealed a significant role of glycosylation profile alterations in the viral glycoproteins - hemagglutinin (HA) and neuraminidase (NA), in the emergence of both seasonal and pandemic strains. Viral antigenic drift can modify the number and location of glycosylation sites, altering a wide range of biological activities and the antigenic properties of the strain. In view of the key role of glycans in determining antigenicity, elucidating the glycosylation profiles of influenza strains is a requirement towards the development of improved vaccines. Sequence-based analysis of viral RNA has provided great insight into the role of glycosite modifications in altering virulence and pathogenicity. Nonetheless, this sequence-based approach can onl

SUBMITTER: Cruz E 

PROVIDER: S-EPMC5861804 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature