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Glycobiology Advance Access originally published online on July 6, 2005
Glycobiology 2005 15(11):1076-1083; doi:10.1093/glycob/cwj004
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

Molecular cloning and functional expression of a novel Helicobacter pylori {alpha}-1,4 fucosyltransferase

Said Rabbani2, Viktoria Miksa2, Beat Wipf3 and Beat Ernst1,2

2 Institute of Molecular Pharmacy, Pharmacenter, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland; and 3 Hoffmann-La Roche, CH-4002 Basel, Switzerland

1 To whom correspondence should be addressed; e-mail: beat.ernst{at}unibas.ch

Received on December 17, 2004; revised on June 23, 2005; accepted on June 23, 2005

Helicobacter pylori is an important human pathogen which causes both gastric and duodenal ulcers and is associated with gastric cancer and lymphoma. This microorganism synthesizes fucosylated oligosaccharides, predominantly the Galb-1,4GlcNAc (Type II) blood group antigens Lewis X and Y, whereas a small population also expresses the Galb-1,3GlcNAc (Type I) blood group antigens Lewis A and B. These carbohydrate structures are known to mimic host cell antigens and permit the bacteria to escape from the host immune response. Here, we report the cloning and characterization of a novel H. pylori {alpha}-1,4 fucosyltransferase (FucT). In contrast to the family members characterized to date, this enzyme shows exclusively Type I acceptor substrate specificity. The enzyme consisting of 432 amino acids (MW 50,502 Da) was cloned using a polymerase chain reaction (PCR)-based approach. It exhibits a high degree of identity (75–87%) and similar structural features, for example, in the heptamer repeat pattern, with other H. pylori FucTs. The kinetic characterization revealed a very efficient transferase (kcat/Km = 229 mM21s21) for the Type I acceptor substrate (Gal)-1,3 GlcNAc-Lem (1). Additionally, the enzyme possesses a broad tolerance toward nonnatural Type I acceptor substrate analogs and therefore represents a valuable tool for the chemoenzymatic synthesis of Lewis A, sialyl Lewis A as well as mimetics thereof.

Key words: enzymatic synthesis / Helicobacter pylori / sialy Lewisa/x and mimetics thereof / {alpha}-1,4 fucosyltransferase


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