N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population
ABSTRACT Glycosylation of the influenza A virus hemagglutinin is crucial for viral fitness and immune evasion. The hemagglutinin of contemporary human A(H3N2) influenza A viruses is extensively glycosylated with up to 13 putative glycosylation sites. Glycan types and occupancy of these sites are not uniform: while most...