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  Lectin-affinity chromatography for downstream processing of current influenza virus strains from MDCK and Vero cell cultivations

Opitz, L., Zimmermann, A., Genzel, Y., Lübben, H., Reichl, U., & Wolff, M. W. (2007). Lectin-affinity chromatography for downstream processing of current influenza virus strains from MDCK and Vero cell cultivations. Poster presented at AIChE Annual meeting 2007, Salt Lake City, USA.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-970B-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-203D-B
Genre: Poster

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 Creators:
Opitz, L.1, Author              
Zimmermann, A.1, Author              
Genzel, Y.1, Author              
Lübben, H., Author
Reichl, U.1, 2, Author              
Wolff, M. W.1, 3, Author              
Affiliations:
1Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738140              
2Otto-von-Guericke-Universität Magdeburg, ou_1738156              
3Otto-von-Guericke-Universität Magdeburg, External Organizations, ou_1738156              

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 Abstract: Influenza is a contagious respiratory tract disease which causes millions of infections worldwide and several hundred thousand of deaths every year. Seasonal prophylactic vaccinations are important to control epidemic outbreaks. In recent years cell culture based influenza vaccine production has been developed replacing conventional production processes using embryonated chicken eggs. In addition to development in upstream processing, new strategies for purification of these cell culture derived antigens are required. As a capturing step, lectin based affinity chromatography was investigated for purification of current influenza strains from cell culture broths. Two topical virus strains (A/Wisconsin/67/2005 (subtype H3N2), B/Malaysia/2506/2004, both from Novartis Behring, Marburg, Germany) and influenza virus A/Puerto Rico/8/34 (H1N1) were produced in MDCK cell cultures and subsequently screened for lectin binding. The alpha-galactose specific Euonymus europaeus lectin (EEL) represented the most suitable ligand for all three virus strains. Using polymer immobilized EEL all investigated influenza viruses could be efficiently captured from MDCK cell culture broths, while the level of contaminating host cell DNA and proteins was highly reduced. Findings suggest that MDCK cell culture derived influenza viruses contain alpha-galactose on their envelope glycoproteins. In contrast, Influenza virus propagated in Vero cells revealed different lectin binding behavior. Here, most favorable binding was achieved by beta-galactose specific Erythrina christagalli lectin (ECL), while EEL could bind only limited amounts of virus. Results demonstrated that lectin affinity chromatography is a valuable capture step for downstream processing of various influenza virus strains. However, the final choice of lectin depended on host cell specific glycosylation of viral proteins. Work is in progress to characterize in detail the binding and purification properties of a reverse genetics derived reassortant H5N1 virus.

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Language(s): eng - English
 Dates: 2007
 Publication Status: Not specified
 Pages: -
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 Rev. Type: -
 Identifiers: eDoc: 332935
Other: OpitzZimmermannGenzelLuebbenReichlWolff2007
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Title: AIChE Annual meeting 2007
Place of Event: Salt Lake City, USA
Start-/End Date: 2007-11-04 - 2007-11-09

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