Canales Mayordomo, María ÁngelesSastre Valera, JavierOrduna, Jose M.Spruit, Cindy M.Perez-Castells, JavierDominguez, GemaBouwman, Kim M.Van der Woude, RoosmarijnCañada, Francisco JavierNycholat, Corwin M.Paulson, James C.Boons, Geert-JanJimenez-Barbero, Jesusde Vries, Robert P.2024-08-292024-08-292023-03-27Canales A, Sastre J, Orduña J M, Spruit C M, Pérez-Castells J, Domínguez G, Bouwman K M, van der Woude R, Cañada F J, Nycholat C M, Paulson J C, Boons G J, Jiménez-Barbero J, de Vries R P2691-370410.1021/jacsau.2c00664https://hdl.handle.net/20.500.14352/107746Influenza 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.engjournal articlehttps://pubs.acs.org/doi/10.1021/jacsau.2c00664open access54616.921.5influenza virusN-glycanrecognitionglycan arrayNMRCiencias23 Química