The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity
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- 作者：Robert P. de Vries ; Erik de Vries ; Berend Jan Bosch ; Raoul J. de Groot ; Peter J.M. Rottier ; Cornelis A.M. de Haan
- 关键词：Influenza A virus ; Hemagglutinin ; Expression system ; N-linked glycosylation ; Receptor specificity ; Sialic acid ; Glycan-array
- 刊名：Virology
- 出版年：2010
- 出版时间：20 July 2010
- 年：2010
- 卷：403
- 期：1
- 页码：17-25
- 全文大小：944 K
文摘
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.