Adsorptive mutation and N-linked glycosylation modulate influenza virus antigenicity and fitness.

ABSTRACT: Influenza viruses have an error-prone polymerase complex that facilitates a mutagenic environment. Antigenic mutants swiftly arise from this environment with the capacity to persist in both humans and economically important livestock even in the face of vaccination. Furthermore, influenza viruses can adjust the antigenicity of the haemagglutinin (HA) protein, the primary influenza immunogen, using one of four molecular mechanisms. Two prominent mechanisms are: (1) enhancing binding avidity of HA toward cellular receptors to outcompete antibody binding and (2) amino acid substitutions that introduce an N-linked glycan on HA that sterically block antibody binding. In this study we investigate the impact that adsorptive mutation and N-linked glycosylation have on receptor-binding, viral fitne

SUBMITTER: Sealy JE 

PROVIDER: S-EPMC7738305 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature