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  Impact of Influenza Virus Adaptation Status on HA N-Glycosylation Patterns in Cell Culture-Based Vaccine Production

Rödig, J., Rapp, E., Djeljadini, S., Lohr, V., Genzel, Y., Jordan, I., et al. (2011). Impact of Influenza Virus Adaptation Status on HA N-Glycosylation Patterns in Cell Culture-Based Vaccine Production. Journal of Carbohydrate Chemistry, 30(4-6), 281-290. doi:10.1080/07328303.2011.604454.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-8D7D-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-A330-3
Genre: Journal Article

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 Creators:
Rödig, J.1, Author              
Rapp, E.1, Author              
Djeljadini, S.1, Author              
Lohr, V.1, Author              
Genzel, Y.1, Author              
Jordan, I.2, Author
Sandig, V.2, Author
Reichl, U.1, 3, Author              
Affiliations:
1Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738140              
2ProBioGen AG Berlin, Germany, ou_persistent22              
3Otto-von-Guericke-Universität Magdeburg, ou_1738156              

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Free keywords: influenza A virus, virus adaptation, hemagglutinin, HA, N-glycosylation
 Abstract: The highly abundant and strongly immunogenic influenza envelope glycoprotein hemagglutinin (HA) represents the main component of influenza vaccines. Human influenza vaccines are typically produced in embryonated chicken eggs. In addition, cell culture-derived vaccine production systems are currently being established. Since characteristics of glycoproteins such as the HA can be significantly influenced by N-glycosylation, the impact of host cells considered for vaccine manufacturing needs to be addressed. In this study MDCK cell-derived influenza A/PR/8/34 (H1N1) virus was adapted over four passages in AGE1.CR.pIX-cells. HA N-glycosylation patterns (normalized capillary electropherograms) were determined and analyzed using capillary gel electrophoresis with laser induced fluorescence detection (each peak represents at least one distinct N-glycan structure). During the adaptation to AGE1.CR.pIX-cells, virus titers 24 hours post infection improved. HA N-glycosylation patterns of MDCK and AGE1.CR.pIX-derived virus particles differed significantly after the first adaptation step. This clearly suggests that the structure of the viral antigens is strongly influenced by the host cell. Furthermore, AGE1.CR.pIX-derived antigens showed a tendency towards small glycans. Differences between glycan patterns of the four successive passages in AGE1.CR.pIX cell were minor, only low variability in relative peak height was noted in the HA N-glycosylation pattern. Copyright Taylor & Francis Group, LLC [accessed November 24th 2011]

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Language(s): eng - English
 Dates: 2011
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 570619
Other: 30/11
DOI: 10.1080/07328303.2011.604454
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Title: Journal of Carbohydrate Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 30 (4-6) Sequence Number: - Start / End Page: 281 - 290 Identifier: -