期刊
GLYCOBIOLOGY
卷 21, 期 9, 页码 1206-1216出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwr054
关键词
glycolipid; lactosyl sphingosine; lyso-GM3; sialyllactosyl sphingosine; sialyltransferase
资金
- NIH [R01GM076360, R01HD065122]
- Alfred P. Sloan Research Fellowship
- Camille Dreyfus Teacher-Scholarship
Pasteurella multocida (Pm) is a multi-species pathogen that causes diseases in animals and humans. Sialyltransferase activity has been detected in multiple Pm strains and sialylation has been shown to be important for the pathogenesis of Pm. Three putative sialyltransferase genes have been identified in Pm genomic strain Pm70. We have reported previously that a Pm0188 gene homolog in Pm strain P-1059 (ATCC 15742) encodes a multifunctional sialyltransferase (PmST1). We demonstrate here that while PmST1 prefers to use oligosaccharides as acceptors, PmST2 encoded by the Pm0508 gene homolog in the same Pm strain is a novel glycolipid alpha 2-3-sialyltransferase that prefers to use lactosyl lipids as acceptor substrates. PmST2 and PmST1 thus complement each other for an efficient synthesis of alpha 2-3-linked sialosides with or without lipid portion. In addition, beta 1-4-linked galactosyl lipids are better PmST2 substrates than beta 1-3-linked galactosyl lipids. PmST2 has been used successfully in the preparative scale synthesis of sialyllactosyl sphingosine (lyso-GM3), which is an important glycolipid and an intermediate for synthesizing more complex glycolipids such as gangliosides.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据