RT Journal Article SR Electronic(1) A1 Wang, Ge A1 Boulton, Peter G. A1 Chan, Nora W. C. A1 Palcic, Monica M. A1 Taylor, Diane E. YR 1999 T1 Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens JF Microbiology, VO 145 IS 11 SP 3245 OP 3253 DO https://doi.org/10.1099/00221287-145-11-3245 PB Microbiology Society, SN 1465-2080, AB Helicobacter pylori lipopolysaccharides (LPS) contain complex carbohydrates known as Lewis antigens which may contribute to the pathogenesis and adaptation of the bacterium. Involved in the biosynthesis of Lewis antigens is an α1,2-fucosyltransferase (FucT) that adds fucose to the terminal βGal unit of the O-chain of LPS. Recently, the H. pylori (Hp) α1,2-FucT-encoding gene (fucT2) was cloned and analysed in detail. However, due to the low level of expression and instability of the protein, its enzymic activity was not demonstrated. In this study, the Hp fucT2 gene was successfully overexpressed in Escherichia coli. Sufficient amounts of the protein were obtained which revealed α1,2-fucosyltransferase activity to be associated with the protein. A series of substrates were chosen to examine the acceptor specificity of Hp α1,2-FucT, and the enzyme reaction products were identified by capillary electrophoresis. In contrast to the normal mammalian α1,2-FucT (H or Se enzyme), Hp α1,2-FucT prefers to use Lewis X [βGal1-4(αFuc1-3)βGlcNAc] rather than LacNAc [βGal1-4βGlcNAc] as a substrate, suggesting that H. pylori uses a novel pathway (via Lewis X) to synthesize Lewis Y. Hp α1,2-FucT also acts on type 1 acceptor [βGal1-3βGlcNAc] and Lewis a [βGal1-3(αFuc1–4)βGlcNAc], which provides H. pylori with the potential to synthesize H type 1 and Lewis b epitopes. The ability to transfer fucose to a monofucosylated substrate (Lewis X or Lewis a) makes Hp α1,2-FucT distinct from normal mammalian α1,2-FucT., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-145-11-3245