Two Paralogous Gb3/Cd77 Synthases In Birds Show Different Preferences For Their Glycoprotein And Glycosphingolipid Substrates
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES(2021)
摘要
Most glycosyltransferases show remarkable gross and fine substrate specificity, which is reflected in the old one enzyme-one linkage paradigm. While human Gb3/CD77 synthase is a glycosyltransferase that synthesizes the Gal alpha 1 -> 4Gal moiety mainly on glycosphingolipids, its pigeon homolog prefers glycoproteins as acceptors. In this study, we characterized two Gb3/CD77 synthase paralogs found in pigeons (Columba livia). We evaluated their specificities in transfected human teratocarcinoma 2102Ep cells by flow cytofluorometry, Western blotting, high-performance thin-layer chromatography, mass spectrometry and metabolic labelling with C-14-galactose. We found that the previously described pigeon Gb3/CD77 synthase (called P) can use predominately glycoproteins as acceptors, while its paralog (called M), which we serendipitously discovered while conducting this study, efficiently synthesizes Gal alpha 1 -> 4Gal caps on both glycoproteins and glycosphingolipids. These two paralogs may underlie the difference in expression profiles of Gal alpha 1 -> 4Gal-terminated glycoconjugates between neoavians and mammals.
更多查看译文
关键词
Gb3, CD77 synthase, glycosyltransferase, Shiga toxin, birds
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要