Journal
GLYCOBIOLOGY
Volume 25, Issue 12, Pages 1441-1453Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwv060
Keywords
Bombyx mori; glycosylation; sialyltransferase
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Funding
- Agri-Genome Project of the Ministry of Agriculture, Forestry and Fisheries of Japan
- Scientific technique research promotion program for agriculture, forestry, fisheries and food industry
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N-Glycosylation is an important post-translational modification in most secreted and membrane-bound proteins in eukaryotic cells. However, the insect N-glycosylation pathway and the potentials contributing to the N-glycan synthesis are still unclear because most of the studies on these subjects have focused on mammals and plants. Here, we identified Bombyx mori sialyltransferase (BmST), which is a Golgi-localized glycosyltransferase and which can modify N-glycans. BmST was ubiquitously expressed in different organs and in various stages of development and localized at the Golgi. Biochemical analysis using Sf9-expressed BmST revealed that BmST encoded alpha 2,6-sialyltransferase and transferred N-acetylneuraminic acid (NeuAc) to the nonreducing terminus of Gal beta 1-R, but exhibited the highest activity toward GalNAc beta 1,4-GlcNAc-R. Unlike human alpha 2,6-sialyltransferase, BmST required the post-translational modification, especially N-glycosylation, for its full activity. N-Glyco-protein analysis of B. mori fifth instar larvae revealed that high-mannose-type structure was predominant and GlcNAc-linked and fucosylated structures were observed but endogenous galactosyl-, N-acetylgalactosaminyl- and sialyl-N-glycoproteins were undetectable under the standard analytical approach. These results indicate that B. mori genome encodes an alpha 2,6-sialyltransferase, but further investigations of the sialylation potentials are necessary.
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