Qian W, Liu Y, Zhang C, Niu Z, Song H, Qiu B
Expression of bovine follicle stimulating hormone subunits in a Hansenula polymorpha expression system increases the secretion and bioactivity in vivo. [JOURNAL ARTICLE]
Protein Expr Purif 2009 Jul 24.
Bovine follicle-stimulating hormone (bFSH), a pituitary gonadotropin, is a heterodimer hormone that consists of a common alpha subunit non-covalently associated with the hormone-specific beta subunit. Unfortunately, expression levels of recombinant bFSH or its subunits are invariably low. We report here the secretory expression of biologically active bFSHalpha and bFSHbeta subunit in the methylotrophic yeast Hansenula polymorpha. A slightly higher level of expression of recombinant bFSH subunits was achieved by using the Saccharomyces cerevisiae-derived calnexin (ScCne1) as a chaperone in engineered H. polymorpha strains. The preliminary data also suggested that bFSH subunits expressed in H. polymorpha appeared to be less glycosylated. This isoform had been shown to be 80% increase in in vivo bioactivity compared with the hyperglycosylated Pichia pastoris-derived recombinant bFSHalpha/beta. More sophisticated applications of bFSH would profit from the assembled less-glycosylated heterodimer.
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