Authors: Ronaldo Z Mendonça Katia N Greco Roberto H P Moraes Renato M Astray M Barral
Publish Date: 2009/10/20
Volume: 60, Issue: 1-3, Pages: 143-
Abstract
Gene expression in insect cells is an advantageous system for recombinant protein production mainly because of its capacity to produce complex proteins with correct posttranslational modifications Recently we identified and purified a protein from Lonomia obliqua hemolymph able to increase the production of rabies virus glycoprotein expressed in Drosophila melanogaster cells by about 60 In this work the kinetic parameters for cell growth and recombinant rabies virus glycoprotein production were determined in cultures of transfected Drosophila melanogaster Schneider 2 S2 cells expressing recombinant rabies virus glycoprotein rRVGP enriched and nonenriched with the hemolymph of Lonomia obliqua Hb The highest concentration of rRVGP was achieved at the beginning of the culture enriched with Hb indicating that the cells produce greater amounts of rRVGP per cell specific rRVGP concentration at the early exponential growth phase After day 8 a decrease in the concentration of rRVGP ng/mL was observed probably due to protein decomposition The average specific rRVGP production rate μrRVGP was 30 ng rRVGP/107cellday higher than that observed in the nonenriched culture
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