Co-expression of human protein disulfide isomerase (hPDI) enhances secretion of bovine follicle-stimulating hormone (bFSH) in Pichia pastoris.
Bovine follicle-stimulating hormone (bFSH) is a pituitary gonadotropin composed of two non-covalently associated polypeptide subunits, which must be glycosylated, folded, and assembled as a heterodimer to be biologically active. Low-level expression of the recombinant bFSH is the factor that limits its usefulness as a superovulation treatment for cows. To increase the production of recombinant bFSH, human protein disulfide isomerase (hPDI) was expressed simultaneously in engineered Pichia strains. The secretion characteristics of bFSH with or without hPDI were examined. The co-expression of bFSH and hPDI is increased to 1.56 mg/l of heterodimer in the culture medium, which is 6-fold higher when compared with the control strain carrying the bFSH gene only. These results may be generally applicable to increase the expression of other glycoprotein hormones in yeast.
Huo
Xiangdong
X
College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, China.
Liu
Yueyong
Y
Wang
Xu
X
Ouyang
Pingkai
P
Niu
Zhengdong
Z
Shi
Yuhu
Y
Qiu
Bingsheng
B
D000818:Animals; D001483:Base Sequence; D001681:Biological Assay; D015153:Blotting, Western; D002417:Cattle; D005260:Female; D005640:Follicle Stimulating Hormone / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D008969:Molecular Sequence Data; D010053:Ovary / Q000187:drug effects; D010843:Pichia / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000096:biosynthesis*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism
D011994:Recombinant Proteins; D005640:Follicle Stimulating Hormone; D019704:Protein Disulfide-Isomerases