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Glycobiology, 2002, Vol. 12, No. 3 217-228
© 2002 Oxford University Press

Several polylactosamine-modifying glycosyltransferases also use internal GalNAcß1-4GlcNAc units of synthetic saccharides as acceptors

Hanna Salo1,3, Olli Aitio3, Kristiina Ilves3, Eija Bencomo3, Suvi Toivonen3, Leena Penttilä3, Ritva Niemelä3, Heidi Salminen3, Eckart Grabenhorst4, Risto Renkonen5,6 and Ossi Renkonen2,3,5,7

3Institute of Biotechnology, Laboratory of Glycobiology, FIN-00014 University of Helsinki, Finland; 4Protein Glycosylation, Gesellschaft für Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany; 5Rational Drug Design Program, Biomedicum Helsinki, PB 63, FIN-00014 University of Helsinki, Finland; 6Department of Bacteriology and Immunology, Haartman Institute, FIN-00014 University of Helsinki, Finland; and 7Department of Biological Sciences, Division of General Microbiology, FIN-00014 University of Helsinki, Finland

The GalNAcß1-4GlcNAc determinant (LdN) occurs in some human and bovine glycoconjugates and also in lower vertebrates and invertebrates. It has been found in unsubstituted as well as terminally substituted forms at the distal end of conjugated glycans, but it has not been reported previously at truly internal positions of polylactosamine chains. Here, we describe enzyme-assisted conversion of LdNß1-OR oligosaccharides into GlcNAcß1-3GalNAcß1-4GlcNAcß1-OR. The extension reactions, catalyzed by human serum, were modeled after analogous ß3-GlcNAc transfer processes that generate GlcNAcß1-3Galß1-4GlcNAcß1-OR. The newly synthesized GlcNAcß1-3GalNAc linkages were unambiguously identified by nuclear magnetic resonance data, including the appropriate long-range correlations in heteronuclear multiple bond correlation spectra. The novel GlcNAcß1-3'LdN determinant proved to be a functional acceptor for several mammalian glycosyltransferases, suggesting that human polylactosamines may contain internal LdN units in many distinct forms. The GlcNAcß1-3'LdN determinant was unusually resistant toward jackbean ß-N-acetylhexosaminidase; the slow degradation should lead to a convenient method for the search of putative internal LdN determinants in natural polylactosamine chains.

1 Present address: Institute of Biotechnology, Research Program in Cellular Biotechnology, Yeast Laboratory, FIN-00014 University of Helsinki, Finland

2 To whom correspondence should be addressed at Rational Drug Design Program, Biomedicum Helsinki


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