Post-translational modifications of Epstein-Barr virus BARF1 oncogene-encoded polypeptide
Post-translational modifications of Epstein-Barr virus BARF1 oncogene-encoded polypeptide
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DOI：
10.1099/vir.0.83058-0
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发表时间：
2007-10-01
影响因子：
3.8
通讯作者：
Ooka, Tadamasa
中科院分区：
文献类型：
--
作者：
de Turenne-Tessier, Mireille;Ooka, Tadamasa
EB病毒与几种人类淋巴瘤和癌相关，其BARF 1癌基因编码一种被认为在致癌作用中起重要作用的蛋白质。BARF 1重组腺病毒表达系统使我们发现了天然状态下巴尔R蛋白的切割和分泌形式的大分子大小及其在培养物中对各种细胞系的促有丝分裂能力，该系统被用于进一步研究BARF 1蛋白的结构和成熟。我们最近报道了生物物理学研究，显示基于二聚体的寡聚化的巴尔多肽。在这里，新的数据，证实了翻译后修饰预测的巴尔序列：磷酸化丝氨酸和苏氨酸，N-和O-糖基化。对N-和O-聚糖进行了部分表征，并证明这两种修饰都是通过经典途径主动分泌BARF 1蛋白所必需的。
Epstein-Barr virus is associated with several human lymphomas and carcinomas, and its BARF1 oncogene encodes a protein that is thought to play an important role in carcinogenesis. A BARF1 recombinant adenovirus expression system, which led us to discover the macromolecular size of the cleaved and secreted form of the BARR protein in the native state and its mitogenic capacity on various cell lines in culture, was used further to investigate the structure and maturation of the BARF1 protein. We recently reported biophysical studies that showed dimer-based oligomerization of the BARR polypeptide. Here, new data are presented that confirm post-translational modifications predicted from the BARR sequence: phosphorylation on serine and threonine, and N- and O-glycosylation. The N- and O-glycans were partially characterized and it was demonstrated that both modifications are required for active secretion of the BARF1 protein via the classical pathway.