tetano
Editor, Senior Moderator
Microbiol Immunol. 2020 Jan 14. doi: 10.1111/1348-0421.12773. [Epub ahead of print] [h=1]E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens.[/h]
Kikutani Y[SUP]1[/SUP], Okamatsu M[SUP]1[/SUP], Nishihara S[SUP]2[/SUP], Takase-Yoden S[SUP]2[/SUP], Hiono T[SUP]1,[/SUP][SUP]3[/SUP], de Vries RP[SUP]4[/SUP], McBride R[SUP]5[/SUP], Matsuno K[SUP]1,[/SUP][SUP]6[/SUP], Kida H[SUP]6,[/SUP][SUP]7[/SUP], Sakoda Y[SUP]1,[/SUP][SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Avian influenza viruses (AIVs) recognize sialic acid linked α2,3 to galactose (SAα2,3Gal) glycans as receptors. In this study, the interactions between hemagglutinins (HAs) of AIVs and sulfated SAα2,3Gal glycans were analyzed in order to clarify the molecular basis of interspecies transmission of AIVs from ducks to chickens. It was revealed that E190V and N192D substitutions of the HA increased the recovery of viruses derived from an H6 duck virus isolate, A/duck/Hong Kong/960/1980 (H6N2), in chickens. Recombinant HAs from an H6 chicken virus, A/chicken/Tainan/V156/1999 (H6N1), bound to sulfated SAα2,3Gal glycans, whereas the HAs from an H6 duck virus did not. Binding preference of mutant HAs revealed that an E190V substitution is critical for the recognition of sulfated SAα2,3Gal glycans. These results suggest that the binding of the HA from H6 AIVs to sulfated SAα2,3Gal glycans explains a part of mechanisms of interspecies transmission of AIVs from ducks to chickens. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] Avian influenza virus; Hemagglutinin; Interspecies transmission; Sialic acid receptor; Sulfated glycans
PMID: 31943329 DOI: 10.1111/1348-0421.12773
Kikutani Y[SUP]1[/SUP], Okamatsu M[SUP]1[/SUP], Nishihara S[SUP]2[/SUP], Takase-Yoden S[SUP]2[/SUP], Hiono T[SUP]1,[/SUP][SUP]3[/SUP], de Vries RP[SUP]4[/SUP], McBride R[SUP]5[/SUP], Matsuno K[SUP]1,[/SUP][SUP]6[/SUP], Kida H[SUP]6,[/SUP][SUP]7[/SUP], Sakoda Y[SUP]1,[/SUP][SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Avian influenza viruses (AIVs) recognize sialic acid linked α2,3 to galactose (SAα2,3Gal) glycans as receptors. In this study, the interactions between hemagglutinins (HAs) of AIVs and sulfated SAα2,3Gal glycans were analyzed in order to clarify the molecular basis of interspecies transmission of AIVs from ducks to chickens. It was revealed that E190V and N192D substitutions of the HA increased the recovery of viruses derived from an H6 duck virus isolate, A/duck/Hong Kong/960/1980 (H6N2), in chickens. Recombinant HAs from an H6 chicken virus, A/chicken/Tainan/V156/1999 (H6N1), bound to sulfated SAα2,3Gal glycans, whereas the HAs from an H6 duck virus did not. Binding preference of mutant HAs revealed that an E190V substitution is critical for the recognition of sulfated SAα2,3Gal glycans. These results suggest that the binding of the HA from H6 AIVs to sulfated SAα2,3Gal glycans explains a part of mechanisms of interspecies transmission of AIVs from ducks to chickens. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] Avian influenza virus; Hemagglutinin; Interspecies transmission; Sialic acid receptor; Sulfated glycans
PMID: 31943329 DOI: 10.1111/1348-0421.12773