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J. Biol. Chem., Vol. 278, Issue 24, 21893-21900, June 13, 2003

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C-terminal Amino Acids of Helicobacter pylori 1,3/4 Fucosyltransferases Determine Type I and Type II Transfer^*,

Bing Ma , Ge Wang  , Monica M. Palcic ¶, Bart Hazes  || and Diane E. Taylor  **

From the Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada, ^¶ Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada

The 1,3/4 fucosyltransferase (FucT) enzyme from Helicobacter pylori catalyzes fucose transfer from donor GDP--L-fucose to the GlcNAc group of two series of acceptor substrates in H. pylori lipopolysaccharide: Gal1,3GlcNAc (Type I) or Gal1,4GlcNAc (Type II). Fucose is added either in 1,3 linkage of Type II acceptor to produce Lewis X or in 1,4 linkage of Type I acceptor to produce Lewis A, respectively. H. pylori FucTs from different strains have distinct Type I or Type II substrate specificities. FucT in H. pylori strain NCTC11639 has an exclusive 1,3 activity because it recognizes only Type II substrates, whereas FucT in H. pylori strain UA948 can utilize both Type II and Type I acceptors; thus it has both 1,3 and 1,4 activity, respectively. To identify elements conferring substrate specificity, 12 chimeric FucTs were constructed by domain swapping between 11639FucT and UA948FucT and characterized for their ability to transfer fucose to Type I and Type II acceptors. Our results indicate that the C-terminal region of H. pylori FucTs controls Type I and Type II acceptor specificity. In particular, the highly divergent C-terminal portion, seven amino acids DNPFIFC at positions 347–353 in 11639FucT, and the corresponding 10 amino acids CNDAHYSALH at positions 345–354 in UA948FucT, controls the Type I and Type II acceptor recognition. This is the opposite of mammalian FucTs where acceptor preference is determined primarily by the N-terminal residues in the hypervariable stem domain.

Received for publication, February 19, 2003 , and in revised form, March 27, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AAF35291.

^* This work was supported by funding from the Canadian Bacterial Diseases Network Center of Excellent Program (to D. E. T.) and the National Sciences and Engineering Research Council (to M. M. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental data.

Present address: Dept. of Microbiology, University of Georgia, Athens, GA 30602.

^|| Medical Scholar with the Alberta Heritage Foundation for Medical Research.

^** Medical Scientist with the Alberta Heritage Foundation for Medical Research. To whom correspondence should be addressed: Dept. of Medical Microbiology and Immunology, 1-28 Medical Sciences Building, University of Alberta, Edmonton, AB T6G 2H7, Canada. Tel.: 780-492-4777; Fax: 780-492-7521; E-mail: diane.taylor{at}ualberta.ca.

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