Journal
VIROLOGY
Volume 403, Issue 1, Pages 17-25Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.03.047
Keywords
Influenza A virus; Hemagglutinin; Expression system; N-linked glycosylation; Receptor specificity; Sialic acid; Glycan-array
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Funding
- Impulse Veterinary Avian Influenza Research in the Netherlands
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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. (C) 2010 Elsevier Inc. All rights reserved.
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