The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity.
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.
de Vries
Robert P
RP
Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
de Vries
Erik
E
Bosch
Berend Jan
BJ
de Groot
Raoul J
RJ
Rottier
Peter J M
PJ
de Haan
Cornelis A M
CA
D000818:Animals; D002460:Cell Line; D006031:Glycosylation; D006389:Hemagglutinins, Viral / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000502:physiology*; D007313:Insecta; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D053585:Virus Attachment
D006389:Hemagglutinins, Viral; C458881:hemagglutinin fusogenic peptide, influenza virus