Gong M, Ooka T, Matsuo T, Kieff E
J Virol. 1987 Feb;61(2):499-508. doi: 10.1128/JVI.61.2.499-508.1987.
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, and B. Roizman, J. Virol. 56:807-813, 1985), has now been shown to encode a 110-kilodalton glycoprotein. Late infectious cycle RNAs of 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.
爱泼斯坦-巴尔病毒DNA开放阅读框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和B.G. Barrell，《自然》[伦敦]310:207 - 211，1984年），通过核苷酸序列比较发现它可能编码一种类似于单纯疱疹病毒gB的蛋白质（P.E. Pellett、M.D. Biggin、B. Barrell和B. Roizman，《病毒学杂志》56:807 - 813，1985年），现已证明它编码一种110千道尔顿的糖蛋白。从BALF4转录出3.0和1.8千碱基的晚期感染周期RNA。这些RNA在体外的翻译、BALF4在体外的转录和翻译，或者在衣霉素存在下对细胞进行代谢标记并用BALF4特异性血清进行免疫沉淀，都能鉴定出gp110的93千道尔顿前体。由于N - 糖苷酶F仅将gp110的大小降至105千道尔顿，gp110可能同时具有N - 连接和O - 连接的糖基化，gp110是爱泼斯坦 - 巴尔病毒感染细胞中一种丰富的糖蛋白。在感染的淋巴细胞和从重组表达载体表达该基因的3T3细胞中，大部分蛋白质位于细胞质和核周。与gB不同，在感染细胞的质膜中未检测到gp110。在复制爱泼斯坦 - 巴尔病毒的细胞中，gp110定位于内核膜和外核膜板层以及有时含有包膜病毒的内质网结构。gp110可能在修饰受感染的细胞内膜方面发挥重要作用。
