2 MAJOR OUTER ENVELOPE GLYCOPROTEINS OF EPSTEIN-BARR VIRUS ARE ENCODED BY THE SAME GENE
2 MAJOR OUTER ENVELOPE GLYCOPROTEINS OF EPSTEIN-BARR VIRUS ARE ENCODED BY THE SAME GENE
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DOI：
10.1128/jvi.54.3.665-674.1985
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发表时间：
1985-01-01
影响因子：
5.4
通讯作者：
KIEFF, E
中科院分区：
文献类型：
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作者：
BEISEL, C;TANNER, J;KIEFF, E
已知Epstein-Barr病毒的两种主要外包膜糖蛋白gp 350和gp 220由3.2-和2.5-内切酶RNA种类编码，其映射到相同的DNA片段。这些RNA种类具有相同的5“和3”末端。较大的RNA由2777个碱基的DNA片段编码，该DNA片段之前是TATTAAA，在其3“端附近具有AATAAA，并包含2721个碱基的开放阅读框架。较小的RNA有一个内部剪接，它保持相同的开放阅读框架。翻译的3.2-和2.5-核糖核酸酶RNA种类产生的蛋白质的135和100千道尔顿。开放阅读框的907个密码子和gp 350前体的135千道尔顿大小之间的差异是由于蛋白质在凝胶电泳中的异常行为，因为从大肠杆菌中的大多数EB病毒开放阅读框翻译的蛋白质具有相似的性质。用兔抗E. coli特异性免疫沉淀gp 350和gp 220，证实了定位和测序结果，以及翻译阅读框架。兔抗血清还与复制病毒和中和病毒的细胞的质膜反应，特别是在加入补体后。这是首次证明gp 350和gp 220的一级氨基酸序列具有可诱导中和抗体的表位。基于对gp 350蛋白一级序列的理论分析，提出了一个gp 350蛋白的模型。
Two major outer envelope glycoproteins of Epstein-Barr virus, gp350 and gp220, are known to be encoded by 3.2- and 2.5-kilobase RNA species which map to the same DNA fragment. These RNA species have the same 5'' and 3'' ends. The larger RNA is encoded by a 2777-base DNA segment which is preceded by TATTAAA had AATAAA near its 3'' end, and contained a 2721-base open reading frame. The smaller RNA has one internal splice which maintains the same open reading frame. Translation of the 3.2- and 2.5-kilobase RNA species yielded proteins of 135 and 100 kilodaltons. The discrepancy between the 907 codons of the open reading frame and the 135-kilodalton size of the gp350 precursor is due to anomalous behavior of the protein in gel electrophoresis, since a protein translated from most of the Epstein-Barr virus open reading frame in Escherichia coli had similar properties. Antisera raised in rabbits to the protein expressed in E. coli specifically immunoprecipitated gp350 and gp220, confirming the mapping and sequencing results, and the translational reading frame. The rabbit antisera also reacted with the plasma membranes of cells that were replicating virus and neturalized virus, particularly after the addition of complement. This is the first demonstration that the primary amino acid sequence of gp350 and gp220 has epitopes which can induce neutralizing antibody. A model is proposed for the gp350 protein based on the theoretical analysis of its primary sequence.