The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity

Virology. 2010 Jul 20;403(1):17-25. doi: 10.1016/j.virol.2010.03.047. Epub 2010 May 2.


In this study we evaluated the receptor-binding properties of recombinant soluble hemagglutinin (HA) trimers (subtype H2 and H7) produced in insect S2 cells, human HEK293T or HEK293S GnTI(-) cells, which produce proteins with paucimannose, complex or high-mannose N-linked glycans, respectively. The results show that HA proteins that only differ in their glycosylation status possess different receptor fine specificities. HEK293T cell-produced HA displayed a very narrow receptor specificity. However, when treated with neuraminidase this HA was able to bind more glycans with similar specificity as HEK293S GnTI(-) cell-produced HA. Insect cell-produced HA demonstrated decreased receptor specificity. As a consequence, differences in HA fine receptor specificities could not be observed with the insect cell-, but were readily detected with the HEK293S GnTI(-) cell-produced HAs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Glycosylation
  • Hemagglutinins, Viral / metabolism*
  • Humans
  • Influenza A virus / physiology*
  • Insecta
  • Protein Binding
  • Protein Processing, Post-Translational
  • Virus Attachment*


  • Hemagglutinins, Viral
  • hemagglutinin fusogenic peptide, influenza virus