tetano
Editor, Senior Moderator
JACS Au
. 2023 Feb 17;3(3):868-878.
doi: 10.1021/jacsau.2c00664. eCollection 2023 Mar 27.
Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
Angeles Canales[SUP] 1 [/SUP], Javier Sastre[SUP] 2 [/SUP], Jose M Orduña[SUP] 3 [/SUP], Cindy M Spruit[SUP] 4 [/SUP], Javier Pérez-Castells[SUP] 3 [/SUP], Gema Domínguez[SUP] 3 [/SUP], Kim M Bouwman[SUP] 4 [/SUP], Roosmarijn van der Woude[SUP] 4 [/SUP], Francisco Javier Cañada[SUP] 2 5 [/SUP], Corwin M Nycholat[SUP] 6 [/SUP], James C Paulson[SUP] 6 [/SUP], Geert-Jan Boons[SUP] 4 7 [/SUP], Jesús Jiménez-Barbero[SUP] 5 8 9 10 [/SUP], Robert P de Vries[SUP] 4 [/SUP]
Affiliations
Abstract
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.
. 2023 Feb 17;3(3):868-878.
doi: 10.1021/jacsau.2c00664. eCollection 2023 Mar 27.
Revealing the Specificity of Human H1 Influenza A Viruses to Complex N-Glycans
Angeles Canales[SUP] 1 [/SUP], Javier Sastre[SUP] 2 [/SUP], Jose M Orduña[SUP] 3 [/SUP], Cindy M Spruit[SUP] 4 [/SUP], Javier Pérez-Castells[SUP] 3 [/SUP], Gema Domínguez[SUP] 3 [/SUP], Kim M Bouwman[SUP] 4 [/SUP], Roosmarijn van der Woude[SUP] 4 [/SUP], Francisco Javier Cañada[SUP] 2 5 [/SUP], Corwin M Nycholat[SUP] 6 [/SUP], James C Paulson[SUP] 6 [/SUP], Geert-Jan Boons[SUP] 4 7 [/SUP], Jesús Jiménez-Barbero[SUP] 5 8 9 10 [/SUP], Robert P de Vries[SUP] 4 [/SUP]
Affiliations
- PMID: 37006776
- PMCID: PMC10052259
- DOI: 10.1021/jacsau.2c00664
Abstract
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.