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

Robert P de Vries; Erik de Vries; Berend Jan Bosch; Raoul J de Groot; Peter J M Rottier; Cornelis A M de Haan

doi:10.1016/j.virol.2010.03.047

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

Robert P de Vries, Erik de Vries, Berend Jan Bosch, Raoul J de Groot, Peter J M Rottier, Cornelis A M de Haan

Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	17-25
Number of pages	9
Journal	Virology
Volume	403
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2010.03.047
Publication status	Published - 20 Jul 2010

Bibliographical note

Keywords

Animals
Cell Line
Glycosylation
Hemagglutinins
Humans
Influenza A virus
Insects
Protein Binding
Protein Processing
Virus Attachment
Post-Translational

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title = "The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity",

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.",

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AU - de Vries, Robert P

AU - de Vries, Erik

AU - Bosch, Berend Jan

AU - de Groot, Raoul J

AU - Rottier, Peter J M

AU - de Haan, Cornelis A M

PY - 2010/7/20

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AB - 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.

KW - Animals

KW - Cell Line

KW - Glycosylation

KW - Hemagglutinins

KW - Humans

KW - Influenza A virus

KW - Insects

KW - Protein Binding

KW - Protein Processing

KW - Virus Attachment

KW - Post-Translational

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VL - 403

SP - 17

EP - 25

JO - Virology

JF - Virology

IS - 1

ER -

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

Abstract

Bibliographical note

Keywords

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