Identification of a sialate o-acetyltransferase from Campylobacter jejuni -: Demonstration of direct transfer to the C-9 position of terminal α-2,8-linked sialic acid
Identification of a sialate o-acetyltransferase from Campylobacter jejuni -: Demonstration of direct transfer to the C-9 position of terminal α-2,8-linked sialic acid
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DOI：
10.1074/jbc.m512183200
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发表时间：
2006-04-28
影响因子：
4.8
通讯作者：
Gilbert, M
中科院分区：
文献类型：
--
作者：
Houliston, RS;Endtz, HP;Gilbert, M
我们已经在空肠弯曲杆菌的脂寡糖生物合成位点发现了一个唾液酸o-乙酰转移酶。已知具有该位点的菌株产生唾液化的外核结构，模仿宿主神经节苷，并与引发格林-巴利综合征有关。在大肠杆菌中克隆并表达的乙酰转移酶是可溶的，与o -乙酰转移酶家族的NodL-LacA-CysE成员同源。该酶催化o -乙酰基转移到寡糖结合的唾液酸上，对末端α 2,8-连接残基具有高特异性。这种修饰是针对C-9而不是C-7的，因为人们认为C-7在其他生物体中更常见。尽管它们在真核生物和原核生物中广泛存在和重要，但这是第一个描述纯化唾液酸酯o -乙酰转移酶特性的报告。
We have identified a sialate O-acetyltransferase in the lipo-oligosaccharide biosynthesis locus of Campylobacter jejuni. Strains possessing this locus are known to produce sialylated outer core structures that mimic host gangliosides, and have been implicated in triggering the onset of Guillain-Barre syndrome. The acetyltransferase, which was cloned and expressed as a fusion construct in Escherichia coli, is soluble and homologous with members of the NodL-LacA-CysE family of O-acetyltransferases. This enzyme catalyzes the transfer of O-acetyl groups onto oligosaccharide-bound sialic acid, with a high specificity for terminal alpha 2,8-linked residues. The modification is directed to C-9 and not C-7 as is believed to occur more commonly in other organisms. Despite their wide prevalence and importance in both eukaryotes and prokaryotes, this is the first report to describe the characterization of a purified sialate O-acetyltransferase.