Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae

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Abstract
Here we studied the glycosylation of a mammalian protein, the ectodomain of rat nerve growth factor receptor (NGFR e ), in Saccharomyces cerevisiae. NGFR e is secreted to the culture medium of S. cerevisiae if it is fused to a polypeptide (hsp150Δ) carrier. The hsp150Δ‐carrier has 95 serine and threonine residues, which were extensively O‐glycosylated. In spite of 41 potential sites, NGF e lacked O‐glycans, whether fused to the carrier or not. Distortion of the conformation of NGFR e by inhibition of disulfide formation did not promote O‐glycosylation, whereas N‐glycosylation was enhanced. Thus, the serine and threonine residues of the hsp150Δ‐NGFR e fusion protein were highly selectively O‐glycosylated.