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Glycobiology Advance Access published online on February 20, 2003
Glycobiology, doi:10.1093/glycob/cwg053
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Submitted on December 26, 2002
Revised on January 27, 2003
Accepted on February 5, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Evidence for a sialic acid salvaging pathway in lepidopteran insect cells

Jason Hollister 1, Harald Conradt 2, Donald L. Jarvis 1

1 Department of Molecular Biology, University of Wyoming, Laramie, Wyoming 82071
2 Protein Glycosylation, Gesellschaft fur Biotechnologische Forschung mbH, Braunschweig, Germany

Abstract

We previously described a transgenic insect cell line, Sf{beta}4GalT/ST6 that expresses mammalian {beta}-1,4-galactosyltransferase and {alpha}2,6-sialyltransferase genes and produces glycoproteins with terminally sialylated N-glycans. The ability of these cells to produce sialylated N-glycans was surprising because insect cells contain only small amounts of sialic acid and no detectable CMP-sialic acid. Thus, it was of interest to investigate potential sources of sialic acids for sialoglycoprotein synthesis by these cells. In this study, we found that Sf{beta}4GalT/ST6 cells can produce sialylated N-glycans when cultured in the presence, but not in the absence of fetal bovine serum. The serum component(s) supporting N-glycan sialylation by Sf{beta}4GalT/ST6 cells is relatively large, as it was not removed by dialysis in a 50,000 molecular weight cutoff membrane. Serum-free media supplemented with purified fetuin, but not asialofetuin, supported N-glycan sialylation by Sf{beta}4GalT/ST6 cells. The terminally sialylated N-glycans isolated from fetuin also supported glycoprotein sialylation by Sf{beta}4GalT/ST6 cells. Finally, serum-free medium supplemented with N-acetylneuraminic acid or N-acetylmannosamine supported glycoprotein sialylation by Sf{beta}4GalT/ST6 cells, but to a much lower degree than serum or fetuin. Together, these results provide the first evidence of a sialic acid salvaging pathway in insect cells, which begins to explain how Sf{beta}4GalT/ST6 and other transgenic insect cell lines can sialylate recombinant glycoproteins in the absence of a more obvious source of CMP-sialic acid.


Insect cells, baculovirus expression system, glycoprotein biosynthesis, sialic acids, sialylation
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