Evaluation of the purity of a purified, inactivated hepatitis A vaccine (VAQTA (TM))

Manufacture of VAQTA(TM), an inactivated hepatitis A virus vaccine, include s extensive purification of the intact virus particle to remove endogenous components from the host cell culture lysate as well as compounds introduce d in the upstream purification process. Analysis of the final purified hepa titis A virus product by SDS-PAGE prior to inactivation shows that greater than 95% of the protein in the preparation is found in four protein bands, which have been confirmed to be hepatitis A virus capsid proteins VP0. VP1, VP2 and VP3 based on Western blot and mass spectrometry analyses. Validati on of the manufacturing process and direct analysis of the final product we re used to demonstrate that no other specific host cell-derived components are detected and that process residuals are all below the limits of detecti on of the assays used. Establishment of a rigorous standard of high purity for this product was pursued to minimize the impact of impurities during cl inical development of this product and will facilitate the incorporation of this product into combination vaccines. (C) 1999 Elsevier Science Ltd. All rights reserved.