EPSTEIN-BARR-VIRUS GLYCOPROTEIN HOMOLOGOUS TO HERPES-SIMPLEX VIRUS-GB

EPSTEIN-BARR-VIRUS GLYCOPROTEIN HOMOLOGOUS TO HERPES-SIMPLEX VIRUS-GB
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DOI:
10.1128/jvi.61.2.499-508.1987
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发表时间:
1987-02-01
影响因子:
5.4
通讯作者:
KIEFF, E
KIEFF, E
中科院分区:
医学2区
文献类型:
--
作者:
GONG, M;OOKA, T;KIEFF, E

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EB病毒DNA开放阅读框BALF 4(R. Baer,A. T. Bankier,M. D.比金,P.L.作者声明:John W. J.吉布森,G. Hatfull,G. S.哈德逊,S. C.斯塔奇韦尔角亮片,附。Tuffnell和B。G. Barrell,Nature [伦敦] 310:207-211,1984),其通过核苷酸序列比较可以编码类似于单纯疱疹病毒gB(P.E. Pellett,M. D.比金,B。Barrell,和B. Roizman,J. Virol. 56:807-813,1985),现已显示编码110千道尔顿糖蛋白。从BALF 4转录晚期感染性周期RNA至3.0和1.8内切酶。这些RNA在体外的翻译,BALF 4在体外的转录和翻译,或在衣霉素和BALF 4特异性血清的免疫沉淀存在下的细胞的代谢标记导致在gp 110的93千道尔顿前体的鉴定。由于N-糖苷酶F仅将gp 110的大小降低至105千道尔顿,因此gp 110可能具有N-和O-连接的糖基化。gp 110是Epstein-Barr病毒感染细胞中丰富的糖蛋白。在感染的淋巴细胞和3 T3细胞中,其中基因从重组表达载体表达,大多数蛋白质是细胞质和核周的。与gB相反,gp 110在感染的细胞质膜中未检测到。在复制EB病毒的细胞中,gp 110定位于核膜的内、外板层和有时含有包膜病毒的内质网结构。GP 110可能在修饰感染的细胞内膜中起重要作用。
The Epstein-Barr virus DNA open reading frame BALF4 (R. Baer, A. T. Bankier, M. D. Biggin, P. L. Deininger, P. J. Farrell, T. J. Gibson, G. Hatfull, G. S. Hudson, S. C. Stachwell, C. Sequin, P. S. Tuffnell, and B. G. Barrell, Nature [London] 310:207-211, 1984), which by nucleotide sequence comparison could encode a protein similar to herpes simplex virus gB (P. E. Pellett, M. D. Biggin, B. Barrell, andB. Roizman, J. Virol. 56:807-813, 1985), has now been shown to encode a 110-kilodalton glycoprotein. Late infectious cycle RNAs to 3.0 and 1.8 kilobases are transcribed from BALF4. Translation of these RNAs in vitro, transcription and translation of BALF4 in vitro, or metabolic labeling of cells in the presence of tunicamycin and immunoprecipitation with BALF4-specific sera results in identification of a 93-kilodalton precursor to gp110. Since N-glycosidase F only reduces the size of gp110 to 105 kilodaltons, gp110 probably has both N- and O-linked glycosylation. gp110 is an abundant glycoprotein in Epstein-Barr virus-infected cells. In infected lymphocytes and in 3T3 cells, in which the gene is expressed from a recombinant expression vector, most of the protein is cytoplasmic and perinuclear. In contrast to gB, gp110 was not detected in the infected-cell plasma membrane. In cells replicating Epstein-Barr virus, gp110 localized to the inner and outer nuclear membrane lamellae and to endoplasmic reticulum structures which sometimes contained enveloped virus. gp110 may play an important role in modifying infected intracellular membranes.