tetano
Editor, Senior Moderator
Virology
. 2021 Jun 25;562:29-39.
doi: 10.1016/j.virol.2021.06.008. Online ahead of print.
Sulfated glycans containing NeuAcα2-3Gal facilitate the propagation of human H1N1 influenza A viruses in eggs
Tomomi Ichimiya[SUP] 1 [/SUP], Masatoshi Okamatsu[SUP] 2 [/SUP], Takaaki Kinoshita[SUP] 1 [/SUP], Daiki Kobayashi[SUP] 2 [/SUP], Osamu Ichii[SUP] 3 [/SUP], Naoki Yamamoto[SUP] 2 [/SUP], Yoshihiro Sakoda[SUP] 4 [/SUP], Hiroshi Kida[SUP] 5 [/SUP], Hiroto Kawashima[SUP] 6 [/SUP], Kazuo Yamamoto[SUP] 7 [/SUP], Sayaka Takase-Yoden[SUP] 8 [/SUP], Shoko Nishihara[SUP] 9 [/SUP]
Affiliations
Abstract
When human influenza viruses are isolated and passaged in chicken embryos, variants with amino acid substitutions around the receptor binding site of hemagglutinin (HA) are selected; however, the mechanisms that underlie this phenomenon have yet to be elucidated. Here, we analyzed the receptor structures that contributed to propagation of egg-passaged human H1N1 viruses. The analysis included seasonal and 2009 pandemic strains, both of which have amino acid substitutions of HA found in strains isolated or passaged in eggs. These viruses exhibited high binding to sulfated glycans containing NeuAcα2-3Gal. In MDCK cells overexpressing the sulfotransferase that synthesize Galβ1-4(SO[SUB]3[/SUB][SUP]-[/SUP]-6)GlcNAc, production of human H1N1 viruses was increased up to 90-fold. Furthermore, these sulfated glycans were expressed on the allantoic and amniotic membranes of chicken embryos. These results suggest that 6-sulfo sialyl Lewis X and/or NeuAcα2-3Galβ1-4(SO[SUB]3[/SUB][SUP]-[/SUP]-6)GlcNAc are involved in efficient propagation of human H1N1 viruses in chicken embryos.
Keywords: Egg-adaptation; Hemagglutinin; Influenza virus; Receptor; Sulfated glycan.
. 2021 Jun 25;562:29-39.
doi: 10.1016/j.virol.2021.06.008. Online ahead of print.
Sulfated glycans containing NeuAcα2-3Gal facilitate the propagation of human H1N1 influenza A viruses in eggs
Tomomi Ichimiya[SUP] 1 [/SUP], Masatoshi Okamatsu[SUP] 2 [/SUP], Takaaki Kinoshita[SUP] 1 [/SUP], Daiki Kobayashi[SUP] 2 [/SUP], Osamu Ichii[SUP] 3 [/SUP], Naoki Yamamoto[SUP] 2 [/SUP], Yoshihiro Sakoda[SUP] 4 [/SUP], Hiroshi Kida[SUP] 5 [/SUP], Hiroto Kawashima[SUP] 6 [/SUP], Kazuo Yamamoto[SUP] 7 [/SUP], Sayaka Takase-Yoden[SUP] 8 [/SUP], Shoko Nishihara[SUP] 9 [/SUP]
Affiliations
- PMID: 34246113
- DOI: 10.1016/j.virol.2021.06.008
Abstract
When human influenza viruses are isolated and passaged in chicken embryos, variants with amino acid substitutions around the receptor binding site of hemagglutinin (HA) are selected; however, the mechanisms that underlie this phenomenon have yet to be elucidated. Here, we analyzed the receptor structures that contributed to propagation of egg-passaged human H1N1 viruses. The analysis included seasonal and 2009 pandemic strains, both of which have amino acid substitutions of HA found in strains isolated or passaged in eggs. These viruses exhibited high binding to sulfated glycans containing NeuAcα2-3Gal. In MDCK cells overexpressing the sulfotransferase that synthesize Galβ1-4(SO[SUB]3[/SUB][SUP]-[/SUP]-6)GlcNAc, production of human H1N1 viruses was increased up to 90-fold. Furthermore, these sulfated glycans were expressed on the allantoic and amniotic membranes of chicken embryos. These results suggest that 6-sulfo sialyl Lewis X and/or NeuAcα2-3Galβ1-4(SO[SUB]3[/SUB][SUP]-[/SUP]-6)GlcNAc are involved in efficient propagation of human H1N1 viruses in chicken embryos.
Keywords: Egg-adaptation; Hemagglutinin; Influenza virus; Receptor; Sulfated glycan.