Additive effect of calreticulin and translation initiation factor eIF4E on secreted protein production in the baculovirus expression system

C.Y. Teng, M.M. van Oers, T.Y. Wu

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

The baculovirus expression vector system is widely used for the production of recombinant proteins. However, the yield of membrane-bound or secreted proteins is relatively low when compared with intracellular or nuclear proteins. In a previous study, we had demonstrated that the co-expression of the human chaperones calreticulin (CALR) or ß-synuclein (ß-syn) increased the production of a secreted protein considerably. Asimilar effectwas also seen when co-expressing insect translation initiation factor eIF4E. In this study, different combinations of the three genes were tested (CALR alone, ß- syn+CALR, or ß-syn+CALR+eIF4E) to further improve secretory protein production by assessing the expression level of a recombinant secreted alkaline phosphatase (SEFP). An additional 1.8-fold increment of SEFP production was obtained when cells co-expressed all the three “helper” genes, compared to cells, in which only CALR was co-produced with SEFP. Moreover, the duration of the SEFP production lasted much longer in cells that co-expressed these three “helper” genes, up to 10 dpi was observed. Utilization of this “triple-supporters” containing vector offers significant advantages when producing secreted proteins and is likely to have benefits for the production of viral vaccines and other pharmaceutical products.
Original languageEnglish
Pages (from-to)8505-8516
JournalApplied Microbiology and Biotechnology
Volume97
Issue number19
DOIs
Publication statusPublished - 2013

Keywords

  • virus-like particles
  • ribosome entry site
  • insect cells
  • messenger-rna
  • vector system
  • structural proteins
  • gene-expression
  • infection
  • coexpression
  • chaperone

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