tetano
Editor, Senior Moderator
J Virol. 2019 Nov 27. pii: JVI.01357-19. doi: 10.1128/JVI.01357-19. [Epub ahead of print] [h=1]Breaking the convention: Sialoglycan variants, Co-receptors and Alternative Receptors for Influenza A Virus Entry.[/h]
Karakus U[SUP]1[/SUP], Pohl MO[SUP]1[/SUP], Stertz S[SUP]2[/SUP].
[h=3]Author information[/h] 1 Institute of Medical Virology, University of Zurich, 8057 Zurich, Switzerland. 2 Institute of Medical Virology, University of Zurich, 8057 Zurich, Switzerland stertz.silke@virology.uzh.ch.
[h=3]Abstract[/h] The influenza A virus (IAV) envelope protein haemagglutinin binds α2,6- or α2,3-linked sialic acid as host cell receptor. Bat IAV subtypes H17N10 and H18N11 form an exception to this rule and do not bind sialic acid but enter cells via MHC class II complexes. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein co-receptors and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.
Copyright ? 2019 American Society for Microbiology.
PMID: 31776280 DOI: 10.1128/JVI.01357-19
Karakus U[SUP]1[/SUP], Pohl MO[SUP]1[/SUP], Stertz S[SUP]2[/SUP].
[h=3]Author information[/h] 1 Institute of Medical Virology, University of Zurich, 8057 Zurich, Switzerland. 2 Institute of Medical Virology, University of Zurich, 8057 Zurich, Switzerland stertz.silke@virology.uzh.ch.
[h=3]Abstract[/h] The influenza A virus (IAV) envelope protein haemagglutinin binds α2,6- or α2,3-linked sialic acid as host cell receptor. Bat IAV subtypes H17N10 and H18N11 form an exception to this rule and do not bind sialic acid but enter cells via MHC class II complexes. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein co-receptors and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.
Copyright ? 2019 American Society for Microbiology.
PMID: 31776280 DOI: 10.1128/JVI.01357-19