Cloning and characterisation of the UDP-glucose 4′-epimerase of Trypanosoma cruzi

被引：30

作者：

Roper, JR ^{[1
]}

Ferguson, MA ^{[1
]}

机构：

[1] Univ Dundee, Sch Life Sci, Div Biol Chem & Mol Microbiol, Dundee DD1 5EH, Scotland

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 2003年 / 132卷 / 01期

基金：

英国惠康基金;

关键词：

Trypanosoma cruzi; GALE; UDP-Glc 4 '-epimerase; O-glycosylation; galactose metabolism;

D O I：

10.1016/j.molbiopara.2003.07.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Trypanosoma cruzi incorporates galactose into many of its cell-surface glycoconjugates but it is unable to transport this sugar through its hexose transporter. Epimerisation of UDP-glucose to UDP-galactose by UDP-glucose 4'-epimerase may be the only way that the parasites can obtain galactose. Here, we describe cloning the T. cruzi UDP-Glc 4'-epimerase (TcGALE) gene and show that it is functional by complementing an Escherichia coli epimerase-deficient strain. The T. cruzi GALE gene encodes a 42.4 kDa protein and the recombinant protein expressed in E. coli is a homodimer in solution with a specific activity of 3.8 U mg(-1) and K-m for UDP-Gal of 114 muM. Unlike the human epimerase. T. cruzi UDP-Glc 4'-epimerase is unable to inter-convert UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine. This may explain why T. cruzi initiates O-glycosylation of its abundant GPI-anchored surface mucins via GlcNAcalpha1-O-Thr/Ser rather than the GalNAcalpha1-O-Thr/Ser linkage that is common for mucins from many other eukaryotes. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：47 / 53

页数：7

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