Eisenberg R J, Hydrean-Stern C, Cohen G H
J Virol. 1979 Sep;31(3):608-20. doi: 10.1128/JVI.31.3.608-620.1979.
The type-common CP-1 antigen of herpes simplex virus type 1 (HSV-1) is associated in the infected cell with two components, a 52,000-molecular-weight glycoprotein (gp52 or pD) and a 59,000-molecular-weight glycoprotein (gp59 or D). The larger form (D) is also found in the virion envelope. It was postulated that pD is a precursor of D. We found that pD shared methionine and arginine tryptic peptides with D isolated from infected cell extracts. D isolated from infected extracts had the same trypric methionine peptide profile as D isolated from the virion envelope. Thus, processing of pD to D does not involve any major alterations in polypeptide structure. Furthermore, D did not share tryptic methionine peptides with the other major glycoproteins of HSV-1. Using [2-3H]mannose as a specific glycoprotein label, we found that pD, which is a basic protein (isoelectric point = 8.0) contained a 1,800-molecular-weight oligomannosyl core moiety and was processed by further glycosylation and sialyation to a more acidic and heterogeneous molecule D, which as a molecular weight of at least 59,000.
1型单纯疱疹病毒（HSV - 1）的共同型CP - 1抗原在受感染细胞中与两种成分相关联，一种是分子量为52,000的糖蛋白（gp52或pD），另一种是分子量为59,000的糖蛋白（gp59或D）。较大的形式（D）也存在于病毒体包膜中。据推测，pD是D的前体。我们发现pD与从受感染细胞提取物中分离出的D共享甲硫氨酸和精氨酸胰蛋白酶肽段。从受感染提取物中分离出的D与从病毒体包膜中分离出的D具有相同的胰蛋白酶甲硫氨酸肽谱。因此，pD加工成D并不涉及多肽结构的任何重大改变。此外，D与HSV - 1的其他主要糖蛋白不共享胰蛋白酶甲硫氨酸肽段。使用[2 - 3H]甘露糖作为特异性糖蛋白标记，我们发现pD是一种碱性蛋白（等电点 = 8.0），含有一个分子量为1,800的寡甘露糖核心部分，并通过进一步的糖基化和唾液酸化加工成一个更酸性且异质性的分子D，其分子量至少为59,000。
