Analyses of chicken sialyltransferases related to O-glycosylation

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• 作者：Shunsuke Kidani ; Hidenori Kaneoka ; ^{kaneoka@nubio.nagoya-u.ac.jp" class="auth_mail" title="E-mail the corresponding author} ; Yuya Okuzaki ; Seiya Asai ; Yusuke Kojima^§ ; ; Ken-ichi Nishijima ; Shinji Iijima
• 关键词：Sialyltransferase ; Chicken ; O-Glycosylation ; Transgenic chicken ; Ganglioside
• 刊名：Journal of Bioscience and Bioengineering
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：122
• 期：4
• 页码：379-384
• 全文大小：893 K

文摘

The chicken β-galactoside α2,3-sialyltransferase 1, 2, and 5 (ST3Gal1, 2, and 5) genes were cloned, and their enzymes were expressed in 293FT cells. ST3Gal1 and 2 exhibited enzymatic activities toward galactose-β1,3-N-acetylgalactosamine and galactose-β1,3-N-acetylglucosamine. ST3Gal5 only exhibited activity toward lactosylceramide. ST3Gal1 and 2 and previously cloned ST3Gal3 and 6 transferred CMP-sialic acid to asialofetuin. Reverse-transcription-quantitative PCR indicated that ST3Gal1 was expressed at higher levels in the trachea, lung, spleen, and magnum, and the strong expression of ST3Gal5 was observed in the spleen, magnum, and small and large intestines. ST3Gal1, 5, and 6 were also expressed in the tubular gland cells of the magnum, which secretes egg-white proteins. ST3Gal1, 5, and 6 were expressed in the egg chorioallantoic membrane, in which influenza viruses are propagated for the production of vaccines.