Eberle R, Courtney R J
J Virol. 1980 Sep;35(3):902-17. doi: 10.1128/JVI.35.3.902-917.1980.
The major glycoprotein complex (VP123) of herpes simplex virus type 1 resolved by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis was purified and further fractionated into two major and two minor components by chromatography of the isolated VP123 region on SDS-hydroxylapatite columns. The two major components (gC and gA/gB) were purified free of other polypeptides and used to prepare specific antisera to these glycoproteins. Radioimmune precipitation demonstrated that these antisera were specific for the antigens used in their production. These two antisera as well as an anti-VP123 serum were further characterized by immunoprecipitation, neutralization, and membrane immunofluorescence techniques. Results indicate that both of the major glycoprotein antigens are expressed on the surface of virions as well as on the surface of infected cells.
通过十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶电泳解析的单纯疱疹病毒1型主要糖蛋白复合物（VP123）被纯化，并通过在SDS-羟基磷灰石柱上对分离的VP123区域进行层析进一步分离为两个主要成分和两个次要成分。两种主要成分（gC和gA/gB）被纯化，不含其他多肽，并用于制备针对这些糖蛋白的特异性抗血清。放射免疫沉淀表明，这些抗血清对用于其制备的抗原具有特异性。通过免疫沉淀、中和及膜免疫荧光技术进一步对这两种抗血清以及抗VP123血清进行了表征。结果表明，两种主要糖蛋白抗原均在病毒粒子表面以及感染细胞表面表达。
