N-glycosylation at the receptor binding site drives differences in receptor binding specificity between influenza B virus lineages.

ABSTRACT: Receptor specificity plays a critical role in influenza virus host tropism and pathogenesis. Influenza A and influenza B viruses (FLUAVs and FLUBVs, respectively) utilize N-glycans with terminal sialic acids on glycoproteins decorating the surface of mucosal epithelial cells as receptors for the virus hemagglutinin (HA) protein. For FLUAVs, the specificity of HA binding to distinct sialic acid linkages on host glycans is a major determinant of species specificity. Amino acid motifs and N-linked glycosylation sites influencing FLUAV HA receptor specificity are well defined. In contrast, considerably less is known regarding determinants of FLUBV receptor specificity, despite its significant contribution to the global influenza disease burden and unique restriction for human hosts. To address

SUBMITTER: Page CK 

PROVIDER: S-EPMC12645935 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature