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Glycobiology Advance Access published online on February 16, 2006
Glycobiology, doi:10.1093/glycob/cwj090
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received October 19, 2005
Revised January 30, 2006
Accepted February 10, 2006

Article

Glycosyltransferases Involved in Type 1 Chain and Lewis Antigen Biosynthesis Exhibit Glycan and Core Chain Specificity

Jan Holgersson 1 and Jonas Löfling 1 *

1 Division of Clinical Immunology, Karolinska Institutet, Karolinska University Hospital, Huddinge, Stockholm, Sweden

* To whom correspondence should be addressed.
Jonas Löfling, E-mail: jonas.lofling{at}ki.se


  Abstract

Sialyl Lewis A(SLea), Lewis A (Lea) and Lewis B (Leb) have been studied in many different biological contexts, e.g. in microbial adhesion and cancer. Their biosynthesis is complex and involves {beta}1,3-galactosyltransferases ({beta}3Gal-Ts) and a combined action of {alpha}2- and/or {alpha}4-fucosyltransferases (Fuc-Ts). Further, O-glycans with different core structures have been identified, and the ability of {beta}3Gal-Ts and Fuc-Ts to use these as substrates has not been resolved.

Therefore, to examine the in vivo specificity of enzymes involved in SLea, Lea and Leb synthesis, we have transiently transfected CHO-K1 cells with relevant human glycosyltransferases and on secreted reporter proteins detected the resulting Lewis antigens on N- and O-linked glycans using Western blotting and Le-specific antibodies.

{beta}3Gal-T1, -T2 and -T5 could synthesize type 1 chains on N-linked glycans, but only {beta}3Gal-T5 worked on O-linked glycans. The latter enzyme could use both core 2 and core 3 precursor structures. Furthermore, the specificity of FUT5 and FUT3 in Lea and Leb synthesis was different, with FUT5 fucosylating H type 1 only on core 2, but FUT3 fucosylating H type 1 much more efficient on core 3 than on core 2. Finally, FUT1 and FUT2 were both found to direct {alpha}2-fucosylation on type 1 chains on both N- and O-linked structures.

This knowledge enables us to engineer recombinant glycoproteins with glycan- and core chain-specific Lewis antigen substitution. Such tools will be important for investigations on the fine carbohydrate specificity of Leb-binding lectins such as Helicobacter pylori adhesins and DC-SIGN, and may also prove useful as therapeutics.

Keywords: Blood group antigens/{beta}3-Galactosyltransferase/cancer associated epitopes/Lewis antigens/fucosyltransferase/.
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