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Lectin-affinity chromatography : a novel purification method for cell culture based Influenza vaccine production from the current season 2006/07

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons86422

Opitz,  L.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86531

Zimmermann,  A.
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;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86517

Wolff,  M. W.
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;
Otto-von-Guericke-Universität Magdeburg, External Organizations;

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Zitation

Opitz, L., Zimmermann, A., Genzel, Y., Lübben, H., Reichl, U., & Wolff, M. W. (2007). Lectin-affinity chromatography: a novel purification method for cell culture based Influenza vaccine production from the current season 2006/07. Talk presented at European BioPerspectives 2007. Cologne, Germany. 2007-05-30 - 2007-06-01.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0013-97DC-2
Zusammenfassung
Influenza remains a major public health concern.Strategies to control influenza outbreaks are mainly focused on prophylactic vaccinations in conjunction with antiviral medications. Cell culture based vaccine production becomes more and more important. Hence new downstream processing strategies have to be developed for virus purification. Former studies [1] have shown that the Euonymus europaeus lectin (EEL) is a suitable ligand for an affinity capture step to purify human Influenza A/PR/8/34 virus. For a chromatographic step matrix selection plays an important role. Therefore different matrices for EEL as ligand were screened, including two membranes, polymer and porous glass particles, cellufine and agarose. Comparing virus binding capacities and product recoveries some of the tested materials indicated a favorable capability for virus purification in contrast to cellufine sulfate, an alternative affinity matrix used for virus purification. Most virus binding was achieved by the membranes and the polymer based adsorbent, respectively. Furthermore, membranes have a far higher binding capacity than other tested adsorbents. To determine the general applicability of lectin-affinity chromatography to other influenza viruses additional studies are currently conducted. Therefore, two of the topical viruses from the flu season 2006/07 (A/Wisconsin/67/2005 (H3N2) and B/Malaysia/2506/2004; both produced in MDCK cell culture, Novartis Behring, Marburg) were screened for lectin binding. In addition, the impact of the host cells on purification by lectin-affinity chromatography has been evaluated. Therefore, Influenza A/PR/8/34 virus was propagated in MDCK and Vero cells and screened for ligand binding and afterwards subjected to purification via the most suitable lectins. [1] Opitz,L.et al.2006.Vaccine;doi:10.1016/j.Vaccine.2006.08.043