Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae.
We have expressed fragments of the cDNA coding for mature human interleukin-1 alpha (hIL-1 alpha) in Saccharomyces cerevisiae. Mature hIL-1 alpha contains one potential N-linked glycosylation site that is not recognized in mammalian cells. Translational fusions to either one of three yeast signal sequences resulted in secretion of bioactive, N-glycosylated hIL-1 alpha. The extent of glycosylation was significantly reduced using the alpha-factor signal sequence, which itself contains three N-linked glycosylation sites known to be core glycosylated. N-glycosylation has no effect on biological specific activity.
Department of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406-0939.
G P
GP
Livi
A A
AA
Ferrara
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R
Roskin
P L
PL
Simon
P R
PR
Young
D000595:Amino Acid Sequence; D000818:Animals; D004274:DNA, Recombinant; D005818:Genetic Engineering / Q000379:methods; D006031:Glycosylation; D006801:Humans; D007375:Interleukin-1 / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
D004274:DNA, Recombinant; D007375:Interleukin-1; D021382:Protein Sorting Signals