Abstract
Background Influenza virus is a highly contagious human and animal pathogen causing infections of the respiratory track. Prevention such as high standard hygiene and vaccination still represent the best measures for protection. Beside the traditional egg-based influenza vaccine production, numerous cell culture-based processes are currently being established. Due to its ability to induce strong and protective immune responses, the highly abundant glycoprotein hemagglutinin (HA) represents the major component in influenza vaccines. Since variations in Nglycosylation of glycoproteins such as HA can alter quality characteristics of antigens, the impact of cell lines and process parameters for vaccine manufacturing needs to be addressed. This study investigates the impact of virus adaptation and different harvest time points on HA N-glycosylation. Therefore, the HA of influenza A virus Uruguay/716/2007 (H3N2, high growth reassortant), in the following referred to as IVAUruguay, was purified and N-glycans analyzed by capillary gel electrophoresis with laser-induced fluorescence (CGE-LIF).
Highlights
Influenza virus is a highly contagious human and animal pathogen causing infections of the respiratory track
Cell culture and virus production IVA-Uruguay (H3N2, #07/360, NIBSC, South Mimms, UK) was produced in either adherently growing MDCK (No 84121903) or Vero (No 88020401) cells purchased from ECACC (Salisbury, UK)
Adaptation of the virus to Vero cells resulted in increased virus yields within shorter time frames in the new host system: in the first passage of Vero cells 2.1 HAU were obtained at 96 hpi, whereas in the fifth passage a titer of 2.7 HAU at 72 hpi was reached
Summary
Influenza virus is a highly contagious human and animal pathogen causing infections of the respiratory track. Prevention such as high standard hygiene and vaccination still represent the best measures for protection. Beside the traditional egg-based influenza vaccine production, numerous cell culture-based processes are currently being established. Due to its ability to induce strong and protective immune responses, the highly abundant glycoprotein hemagglutinin (HA) represents the major component in influenza vaccines. Since variations in Nglycosylation of glycoproteins such as HA can alter quality characteristics of antigens, the impact of cell lines and process parameters for vaccine manufacturing needs to be addressed. The HA of influenza A virus Uruguay/716/2007 (H3N2, high growth reassortant), in the following referred to as IVAUruguay, was purified and N-glycans analyzed by capillary gel electrophoresis with laser-induced fluorescence (CGE-LIF)
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