tetano
Editor, Senior Moderator
Sci Rep
. 2022 Feb 8;12(1):2081.
doi: 10.1038/s41598-022-05961-x.
Structural analysis of N-glycans in chicken trachea and lung reveals potential receptors of chicken influenza viruses
Noriko Suzuki[SUP] 1 [/SUP], Tatsuya Abe[SUP] 2 [/SUP], Shunji Natsuka[SUP] 2 3 [/SUP]
Affiliations
Abstract
Although avian influenza A viruses (avian IAVs) bind preferentially to terminal sialic acids (Sia) on glycans that possess Siaα2-3Gal, the actual glycan structures found in chicken respiratory tracts have not been reported. Herein, we analyzed N-glycan structures in chicken trachea and lung, the main target tissues of low pathogenic avian IAVs. 2-Aminopyridine (PA)-labeled N-glycans from chicken tissues were analyzed by combined methods using reversed-phase liquid chromatography (LC), electrospray ionization (ESI)-mass spectrometry (MS), MS/MS, and multistage MS (MS[SUP]n[/SUP]), with or without modifications using exoglycosidases, sialic acid linkage-specific alkylamidation (SALSA), and/or permethylation. The results of SALSA indicated that PA-N-glycans in both chicken trachea and lung harbored slightly more α2,6-Sia than α2,3-Sia. Most α2,3-Sia on N-glycans in chicken trachea was a fucosylated form (sialyl Lewis X, sLe[SUP]x[/SUP]), whereas no sLe[SUP]x[/SUP] was detected in lung. By contrast, small amounts of N-glycans with 6-sulfo sialyl LacNAc were detected in lung but not in trachea. Considering previous reports that hemagglutinins (HAs) of avian IAVs originally isolated from chicken bind preferentially to α2,3-Sia with or without fucosylation and/or 6-sulfation but not to α2,6-Sia, our results imply that avian IAVs do not evolve to possess HAs that bind preferentially to α2,6-Sia, regardless of the abundance of α2,6-Sia.
. 2022 Feb 8;12(1):2081.
doi: 10.1038/s41598-022-05961-x.
Structural analysis of N-glycans in chicken trachea and lung reveals potential receptors of chicken influenza viruses
Noriko Suzuki[SUP] 1 [/SUP], Tatsuya Abe[SUP] 2 [/SUP], Shunji Natsuka[SUP] 2 3 [/SUP]
Affiliations
- PMID: 35136109
- PMCID: PMC8827061
- DOI: 10.1038/s41598-022-05961-x
Abstract
Although avian influenza A viruses (avian IAVs) bind preferentially to terminal sialic acids (Sia) on glycans that possess Siaα2-3Gal, the actual glycan structures found in chicken respiratory tracts have not been reported. Herein, we analyzed N-glycan structures in chicken trachea and lung, the main target tissues of low pathogenic avian IAVs. 2-Aminopyridine (PA)-labeled N-glycans from chicken tissues were analyzed by combined methods using reversed-phase liquid chromatography (LC), electrospray ionization (ESI)-mass spectrometry (MS), MS/MS, and multistage MS (MS[SUP]n[/SUP]), with or without modifications using exoglycosidases, sialic acid linkage-specific alkylamidation (SALSA), and/or permethylation. The results of SALSA indicated that PA-N-glycans in both chicken trachea and lung harbored slightly more α2,6-Sia than α2,3-Sia. Most α2,3-Sia on N-glycans in chicken trachea was a fucosylated form (sialyl Lewis X, sLe[SUP]x[/SUP]), whereas no sLe[SUP]x[/SUP] was detected in lung. By contrast, small amounts of N-glycans with 6-sulfo sialyl LacNAc were detected in lung but not in trachea. Considering previous reports that hemagglutinins (HAs) of avian IAVs originally isolated from chicken bind preferentially to α2,3-Sia with or without fucosylation and/or 6-sulfation but not to α2,6-Sia, our results imply that avian IAVs do not evolve to possess HAs that bind preferentially to α2,6-Sia, regardless of the abundance of α2,6-Sia.