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马疱疹病毒1型的高度O-糖基化糖蛋白gp2由基因71编码。

The highly O-glycosylated glycoprotein gp2 of equine herpesvirus 1 is encoded by gene 71.

作者信息

Wellington J E, Allen G P, Gooley A A, Love D N, Packer N H, Yan J X, Whalley J M

机构信息

School of Biological Sciences, Macquarie University, Sydney, New South Wales, Australia.

出版信息

J Virol. 1996 Nov;70(11):8195-8. doi: 10.1128/JVI.70.11.8195-8198.1996.

Abstract

There have been conflicting reports regarding the gene assignment of the high-molecular-mass envelope glycoprotein gp2 (gp300) of equine herpesvirus 1. Here, we provide an unequivocal demonstration that gp2 is encoded by gene 71. gp2 that was purified with a defining monoclonal antibody was cleaved internally to yield a 42-kDa protein encoded by gene 71. Amino acid composition data and N-terminal sequence analysis of a tryptic peptide identified gp2 as the product of equine herpesvirus 1 gene 71 with the SWISS-PROT database. Analysis of gp2's monosaccharide composition and the 42-kDa subunit showed that the high level of O glycosylation occurs on the serine/threonine-rich region upstream of the cleavage site.

摘要

关于马疱疹病毒1型高分子量包膜糖蛋白gp2(gp300)的基因定位,一直存在相互矛盾的报道。在此,我们提供了明确的证据表明gp2由基因71编码。用一种特异性单克隆抗体纯化的gp2在内部被切割,产生了由基因71编码的42 kDa蛋白。通过胰蛋白酶肽段的氨基酸组成数据和N端序列分析,并与SWISS-PROT数据库比对,确定gp2为马疱疹病毒1型基因71的产物。对gp2的单糖组成和42 kDa亚基的分析表明,高水平的O-糖基化发生在切割位点上游富含丝氨酸/苏氨酸的区域。

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Characterization of human plasma glycoproteins separated by two-dimensional gel electrophoresis.
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