Breaking the Convention: Sialoglycan Variants, Coreceptors, and Alternative Receptors for Influenza A Virus Entry

J Virol. 2020 Jan 31;94(4):e01357-19. doi: 10.1128/JVI.01357-19. Print 2020 Jan 31.

Abstract

The influenza A virus (IAV) envelope protein hemagglutinin binds α2,6- or α2,3-linked sialic acid as a 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 major histocompatibility complex (MHC) class II. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein coreceptors, and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.

Keywords: influenza virus; receptor; viral entry.

Publication types

  • Review

MeSH terms

  • Animals
  • Chiroptera / virology
  • HEK293 Cells
  • Hemagglutinin Glycoproteins, Influenza Virus / metabolism
  • Histocompatibility Antigens Class II / immunology
  • Histocompatibility Antigens Class II / metabolism
  • Humans
  • Influenza A virus / immunology
  • Influenza A virus / metabolism*
  • Influenza A virus / pathogenicity
  • N-Acetylneuraminic Acid / metabolism
  • Neuraminidase / metabolism
  • Receptors, Virus / immunology*
  • Receptors, Virus / metabolism*
  • Virus Attachment
  • Virus Internalization

Substances

  • Hemagglutinin Glycoproteins, Influenza Virus
  • Histocompatibility Antigens Class II
  • Receptors, Virus
  • Neuraminidase
  • N-Acetylneuraminic Acid