| Literature DB >> 20441997 |
Robert P de Vries1, Erik de Vries, Berend Jan Bosch, Raoul J de Groot, Peter J M Rottier, Cornelis A M de Haan.
Abstract
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. Copyright 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID: 20441997 DOI: 10.1016/j.virol.2010.03.047
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616