Oct. 2001, Accessed: Jul. 30, 2014. [Online]. Available: http://www.ncbi.nlm.nih.

gov/pubmed/11536142.

[84] J. M. Young, C. Cheadle, J. S. Foulke, W. N. Drohan, and N. Sarver, “Utilization of

an Epstein-Barr virus replicon as a eukaryotic expression vector,” Gene, vol. 62,

pp. 171–185, 1988, doi: 10.1016/0378-1119(88)90556-2

[85] J. Ye, V. Kober, M. Tellers, Z. Naji, P. Salmon, and J. F. Markusen, “High-level

protein expression in scalable CHO transient transfection,” Biotechnol. Bioeng.,

vol. 103, pp. 542–551, 2009, doi: 10.1002/bit.22265

[86] H. Rodrigues Goulart, F. Dos, S. Arthuso, M. V. N. Capone, T. L. de Oliveira, P.

Bartolini, and C. R. J. Soares, “Enhancement of human prolactin synthesis by so-

dium butyrate addition to serum-free CHO cell culture,” J. Biomed. Biotechnol.,

vol. 2010, p. 405872, Jan. 2010, doi: 10.1155/2010/405872

[87] R. Damiani, B. E. Almeida, J. E. Oliveira, P. Bartolini, and M. T. C. P. Ribela,

“Enhancement of human thyrotropin synthesis by sodium butyrate addition to

serum-free CHO cell culture,” Appl. Biochem. Biotechnol., vol. 171, no. 7,

pp. 1658–1672, Dec. 2013, doi: 10.1007/s12010-013-0467-9

[88] Y. H. Sung, Y. J. Song, S. W. Lim, J. Y. Chung, and G. M. Lee, “Effect of sodium

butyrate on the production, heterogeneity and biological activity of human throm-

bopoietin by recombinant Chinese hamster ovary cells,” J. Biotechnol., vol. 112,

pp. 323–335, 2004, doi: 10.1016/j.jbiotec.2004.05.003

[89] Y. Mimura et al., “Butyrate increases production of human chimeric IgG in CHO-

K1 cells whilst maintaining function and glycoform profile,” J. Immunol. Methods,

vol. 247, pp. 205–216, 2001, doi: 10.1016/S0022-1759(00)00308-2

[90] G. Backliwal, M. Hildinger, I. Kuettel, F. Delegrange, D. L. Hacker, and F. M. Wurm,

“Valproic acid: A viable alternative to sodium butyrate for enhancing protein ex-

pression in Mammalian cell cultures,” Biotechnology, vol. 101, pp. 182–189, 2008,

doi: 10.1002/bit.21882

[91] D. P. Palermo, M. E. DeGraaf, K. R. Marotti, E. Rehberg, and L. E. Post,

“Production of analytical quantities of recombinant proteins in Chinese hamster

ovary cells using sodium butyrate to elevate gene expression,” J. Biotechnol.,

vol. 19, pp. 35–47, 1991, doi: 10.1016/0168-1656(91)90073-5

[92] S. Ansorge, S. Lanthier, J. Transfiguracion, Y. Durocher, O. Henry, and A. Kamen,

“Development of a scalable process for high-yield lentiviral vector production by

transient transfection of HEK293 suspension cultures,” J. Gene Med., vol. 11,

pp. 868–876, 2009, doi: 10.1002/jgm.1370

[93] Z. Jiang and S. T. Sharfstein, “Sodium butyrate stimulates monoclonal antibody

over-expression in CHO cells by improving gene accessibility,” Biotechnol.

Bioeng., vol. 100, pp. 189–194, 2008, doi: 10.1002/bit.21726

[94] S. Wulhfard, L. Baldi, D. L. Hacker, and F. Wurm, “Valproic acid enhances re-

combinant mRNA and protein levels in transiently transfected Chinese hamster ovary

cells,” J. Biotechnol., vol. 148, pp. 128–132, 2010, doi: 10.1016/j.jbiotec.2010.05.003

[95] G. Backliwal, M. Hildinger, S. Chenuet, M. DeJesus, and F. M. Wurm,

“Coexpression of acidic fibroblast growth factor enhances specific productivity and

antibody titers in transiently transfected HEK293 cells,” N. Biotechnol., vol. 25,

pp. 162–166, 2008, doi: 10.1016/j.nbt.2008.08.007

[96] G. Backliwal, M. Hildinger, S. Chenuet, S. Wulhfard, M. De Jesus, and F. M.

Wurm, “Rational vector design and multi-pathway modulation of HEK 293E cells

yield recombinant antibody titers exceeding 1 g/l by transient transfection under

serum-free conditions,” Nucleic Acids Res., vol. 36, no. 15, p. e96, Sep. 2008, doi:

10.1093/nar/gkn423

[97] S. Fan et al., “Valproic acid enhances gene expression from viral gene transfer vectors,”

J. Virol. Methods, vol. 125, pp. 23–33, 2005, doi: 10.1016/j.jviromet.2004.11.023

Recombinant vaccines: Gag-based VLPs

265