Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
Influenza virus infection remains a threat to human health since viral hemagglutinins are constantly drifting, escaping infection and vaccine-induced antibody responses. Viral hemag-glutinins from different viruses display variability in glycan recognition. In this context, recent H3N2 viruses have...
| Autores: | , , , , , , , , , , , , , |
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| Formato: | artículo |
| Fecha de publicación: | 2023 |
| País: | España |
| Recursos: | Universidad del País Vasco |
| Repositorio: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/60920 |
| Acesso em linha: | http://hdl.handle.net/10810/60920 |
| Access Level: | acceso abierto |
| Palavra-chave: | influenza virus N-glycan recognition glycan array NMR |
| Resumo: | Influenza virus infection remains a threat to human health since viral hemagglutinins are constantly drifting, escaping infection and vaccine-induced antibody responses. Viral hemag-glutinins from different viruses display variability in glycan recognition. In this context, recent H3N2 viruses have specificity for alpha 2,6 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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