de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons86452

Rödig,  J.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86442

Rapp,  E.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86277

Djeljadini,  S.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86389

Lohr,  V.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86303

Genzel,  Y.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86448

Reichl,  U.
Otto-von-Guericke-Universität Magdeburg;
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-8D7D-7
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]