Yeast Expression System for Glycoengineering
Yeast expression system is an alternative to prokaryotic and higher eukaryotic expression system since it offers the attributes of speedy growth, ease to manipulate genes and low costing media like for microbes along with post translational modification and secretory expression like in higher eukaryotes. An increasing number of yeast strains are available for protein expression that are said to increase the yield of the protein, improves the affinity tagging of the proteins, reduces protein breakdown, allows the addition of non-native amino acids (Selenomethionine) into the protein and defines the composition of N-glycan in the protein produced. Following are the existing genera of yeast …show more content…
Presence of AOX1 promoter which is strong and controlled by the induction of methanol is used in recombinant antibody production. An amino terminal signal sequence, commonly S. cerevisiae alpha factor, is required for secretory production of antibody which later undergoes proteolytic cleavage by endo-protease KEX2 for proficient release of immunoglobulins. There is limited data regarding expression of a whole immunoglobulin G. Dimeric scFV-Fc antibodies in P. pastoris attained expression levels of 10-30mg/L. YEAST EXPRESSION SYSTEM FOR THE PRODUCTION OF INTERFERON Plasmid containing cDNA of human interferon gamma is kept under the control of 3-phosphoglycerte kinase promoter in the yeast Saccharomyces cerevisiae. The amount of of expression was greater under PGK promoter than just the IFN-γ mRNA. 25 x 10 (6) units per litre culture of active IFN-γ are synthesized in transformed …show more content…
Hyunah Kim, Su Jin Yoo, Hyun Ah Kang. Yeast synthetic biology for the production of recombinant therapeutic protein. DOI: http://dx.doi.org/10.1111/1567-1364.12195 1-16 First published online: 14 January 2015
2. Tillman V. Gerngross. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nature Biotechnology 22, 1409 - 1414 (2004)
Published online: 4 November 2004 |doi:10.1038/nbt1028
3. Thomas Vogi, Franz S Hartner and Anton Glieder. New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris. Current Opinion in Biotechnology, 2013-12-01, Volume 24, Issue 6, Pages 1094-1101, Copyright © 2013 Elsevier Ltd
4. Maleki A, Roohvand F, Tajerzadeh H, Khanahmad H, Nobari MB, Najafabadi AR. High Expression of Methylotrophic Yeast-Derived Recombinant Human Erythropoietin in a pH-Controlled Batch System. Avicenna J Med Biotechnol. 2010 Oct;2(4):197-206
5. C-M. Chen, Y-C. Chang, C-L. Chen and W. T. K. Cheng. High-Level Expression of Growth Hormone in the Methylotropic Yeast and Its Application on Growth Improvement of Fowls. Asian-Aus. J. Anim. Sci. 13 Supplement July 2000 A: 157
6. R. Dernyck, A Singh and D V Goeddel. Expression of the human interferon-gamma cDNA in
Yeast expression system is an alternative to prokaryotic and higher eukaryotic expression system since it offers the attributes of speedy growth, ease to manipulate genes and low costing media like for microbes along with post translational modification and secretory expression like in higher eukaryotes. An increasing number of yeast strains are available for protein expression that are said to increase the yield of the protein, improves the affinity tagging of the proteins, reduces protein breakdown, allows the addition of non-native amino acids (Selenomethionine) into the protein and defines the composition of N-glycan in the protein produced. Following are the existing genera of yeast …show more content…
Presence of AOX1 promoter which is strong and controlled by the induction of methanol is used in recombinant antibody production. An amino terminal signal sequence, commonly S. cerevisiae alpha factor, is required for secretory production of antibody which later undergoes proteolytic cleavage by endo-protease KEX2 for proficient release of immunoglobulins. There is limited data regarding expression of a whole immunoglobulin G. Dimeric scFV-Fc antibodies in P. pastoris attained expression levels of 10-30mg/L. YEAST EXPRESSION SYSTEM FOR THE PRODUCTION OF INTERFERON Plasmid containing cDNA of human interferon gamma is kept under the control of 3-phosphoglycerte kinase promoter in the yeast Saccharomyces cerevisiae. The amount of of expression was greater under PGK promoter than just the IFN-γ mRNA. 25 x 10 (6) units per litre culture of active IFN-γ are synthesized in transformed …show more content…
Hyunah Kim, Su Jin Yoo, Hyun Ah Kang. Yeast synthetic biology for the production of recombinant therapeutic protein. DOI: http://dx.doi.org/10.1111/1567-1364.12195 1-16 First published online: 14 January 2015
2. Tillman V. Gerngross. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nature Biotechnology 22, 1409 - 1414 (2004)
Published online: 4 November 2004 |doi:10.1038/nbt1028
3. Thomas Vogi, Franz S Hartner and Anton Glieder. New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris. Current Opinion in Biotechnology, 2013-12-01, Volume 24, Issue 6, Pages 1094-1101, Copyright © 2013 Elsevier Ltd
4. Maleki A, Roohvand F, Tajerzadeh H, Khanahmad H, Nobari MB, Najafabadi AR. High Expression of Methylotrophic Yeast-Derived Recombinant Human Erythropoietin in a pH-Controlled Batch System. Avicenna J Med Biotechnol. 2010 Oct;2(4):197-206
5. C-M. Chen, Y-C. Chang, C-L. Chen and W. T. K. Cheng. High-Level Expression of Growth Hormone in the Methylotropic Yeast and Its Application on Growth Improvement of Fowls. Asian-Aus. J. Anim. Sci. 13 Supplement July 2000 A: 157
6. R. Dernyck, A Singh and D V Goeddel. Expression of the human interferon-gamma cDNA in