Capture of cell culture-derived influenza virus by lectins: strain independent, but host cell dependent.
Strategies to control influenza outbreaks are focused mainly on prophylactic vaccination. Human influenza vaccines are trivalent blends of different virus subtypes. Therefore and due to frequent antigenic drifts, strain independent manufacturing processes are required for vaccine production. This study verifies the strain independency of a capture method based on Euonymus europaeus lectin-affinity chromatography (EEL-AC) for downstream processing of influenza viruses under various culture conditions propagated in MDCK cells. A comprehensive lectin binding screening was conducted for two influenza virus types from the season 2007/2008 (A/Wisconsin/67/2005, B/Malaysia/2506/2004) including a comparison of virus-lectin interaction by surface plasmon resonance technology. EEL-AC resulted in a reproducible high product recovery rate and a high degree of contaminant removal in the case of both MDCK cell-derived influenza virus types demonstrating clearly the general applicability of EEL-AC. In addition, host cell dependency of EEL-AC was studied with two industrial relevant cell lines: Vero and MDCK cells. However, the choice of the host cell lines is known to lead to different product glycosylation profiles. Hence, altered lectin specificities have been observed between the two cell lines, requiring process adaptations between different influenza vaccine production systems.
Opitz
Lars
L
Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany.
Zimmermann
Anke
A
Lehmann
Sylvia
S
Genzel
Yvonne
Y
Lübben
Holger
H
Reichl
Udo
U
Wolff
Michael W
MW
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism*; D002460:Cell Line; D002522:Chlorocebus aethiops; D004285:Dogs; D009980:Influenza A virus / Q000254:growth & development* / Q000302:isolation & purification*; D009981:Influenza B virus / Q000254:growth & development* / Q000302:isolation & purification*; D037121:Plant Lectins / Q000378:metabolism*; D011485:Protein Binding; D020349:Surface Plasmon Resonance
D023181:Antimicrobial Cationic Peptides; C047161:Evonymous europa lectin; D037121:Plant Lectins