%0 Journal Article
%A Canales Mayordomo, María Ángeles
%A Sastre Valera, Javier
%A Orduna, Jose M.
%A Spruit, Cindy M.
%A Perez-Castells, Javier
%A Dominguez, Gema
%A Bouwman, Kim M.
%A Van der Woude, Roosmarijn
%A Cañada, Francisco Javier
%A Nycholat, Corwin M.
%A Paulson, James C.
%A Boons, Geert-Jan
%A Jimenez-Barbero, Jesus
%A de Vries, Robert P.
%T Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
%D 2023
%@ 2691-3704
%U https://hdl.handle.net/20.500.14352/107746
%X Influenza virus infection remains a threat to human health since viral hemagglutinins are constantly drifting, escaping infection and vaccine-induced antibody responses. Viral hemagglutinins from different viruses display variability in glycan recognition. In this context, recent H3N2 viruses have specificity for α2,6 sialylated branched N-glycans with at least three N-acetyllactosamine units (tri-LacNAc). In this work, we combined glycan arrays and tissue binding analyses with nuclear magnetic resonance experiments to characterize the glycan specificity of a family of H1 variants, including the one responsible for the 2009 pandemic outbreak. We also analyzed one engineered H6N1 mutant to understand if the preference for tri-LacNAc motifs could be a general trend in human-type receptor-adapted viruses. In addition, we developed a new NMR approach to perform competition experiments between glycans with similar compositions and different lengths. Our results point out that pandemic H1 viruses differ from previous seasonal H1 viruses by a strict preference for a minimum of di-LacNAc structural motifs.
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