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Originally published In Press as doi:10.1074/jbc.M007922200 on September 27, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40057-40063, December 22, 2000
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The Acceptor and Site Specificity of alpha 3-Fucosyltransferase V
HIGH REACTIVITY OF THE PROXIMAL AND LOW OF THE DISTAL Galbeta 1-4GlcNAc UNIT IN i-TYPE POLYLACTOSAMINES*

Maria PykäriDagger §, Suvi ToivonenDagger §, Jari NatunenDagger §, Ritva NiemeläDagger , Heidi SalminenDagger , Olli AitioDagger , Minna EkströmDagger , Pinja ParmanneDagger , Mika VälimäkiDagger ||, Jocelyne Alais||, Claudine Augé||, John B. Lowe**Dagger Dagger , Ossi RenkonenDagger , and Risto Renkonen§§¶¶

From the Dagger  Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland, the || Laboratoire de Chimie Organique Multifonctionelle, Université Paris Sud, 91405 Orsay cedex, France, the ** Howard Hughes Medical Institute and the Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0650, and the §§ Haartman Institute, Department of Bacteriology and Immunology, University of Helsinki and the HUCH Laboratory Diagnostics, P.O. Box 21, 00014, Helsinki, Finland

We report here on in vitro acceptor and site specificity of recombinant alpha 3-fucosyltransferase V (Fuc-TV) with 40 oligosaccharide acceptors. Galbeta 1-4GlcNAc (LN) and GalNAcbeta 1-4GlcNAc (LDN) reacted rapidly; Galbeta 1-3GlcNAc (LNB) reacted moderately, and GlcNAcbeta 1-4GlcNAc (N,N'-diacetyl-chitobiose) reacted slowly yet distinctly. In neutral and terminally alpha 3-sialylated polylactosamines of i-type, the reducing end LN unit reacted rapidly and the distal (sialyl)LN group very slowly; the midchain LNs revealed intermediate reactivities. The data suggest that a distal LN neighbor enhances but a proximal LN neighbor reduces the reactivity of the midchain LNs. This implies that Fuc-TV may bind preferably the tetrasaccharide sequence Galbeta 1-4GlcNAcbeta 1-3Galbeta 1-4GlcNAc for transfer at the underlined monosaccharide. Terminal alpha 3-sialylation of i-type polylactosamines almost doubled the reactivities of the LN units at all positions of the chains. We conclude that, in comparison with human Fuc-TIV and Fuc-TIX, Fuc-TV reacted with a highly distinct site specificity with i-type polylactosamines. The Fuc-TV reactivity of free LNB resembled that of LNBbeta 1-3'R of a polylactosamine, contrasting strongly with the dissimilarity of the reactivities of the analogous pair of LN and LNbeta 1-3'R. This observation supports the notion that LN and LNB may be functionally bound at distinct sites on Fuc-TV surface. Our data show that Fuc-TV worked well with a very wide range of LN-glycans, showing weak reactivity only with distal (sialyl)LN units of i-type polylactosamines, biantennary N-glycans, and I branches of polylactosamines.

* This work was supported in part by Research Grants 38042, 40901, 44318, and 41413 from the Academy of Finland, by Research Grants 40057/97 and 40368/99 from Technology Development Center (TEKES), Helsinki, by a Research Grant from Emil Aaltonen Foundation, Tampere, and by funds from Finnish National Graduate School of Bioorganic Chemistry, University of Turku, (to S. T. and J. N.), the Foundation of Jenny and Antti Wihuri and the Finnish Cultural Foundation (to H. S.), and the University Paris Sud and the CNRS (to J. A. and C. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

Present address: Department of Medical Biochemistry, University of Gothenburg, Box 440, 40530 Gothenburg, Sweden.

Dagger Dagger Supported by National Institutes of Health Grant 1PO1 CA71932. Investigator of the Howard Hughes Medical Institute.

¶¶ To whom correspondence should be addressed. E-mail: risto.renkonen@helsinki.fi.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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