Montalvo E A, Grose C
Virology. 1986 Mar;149(2):230-41. doi: 10.1016/0042-6822(86)90124-8.
Varicella-zoster virus (VZV) specifies the formation of several glycoproteins, including a 118,000-Da mature structural product (gp118). The biologic and biochemical properties of gp118 were studied after production of murine monoclonal antibodies to both a lowpassage laboratory strain (VZV-32) and an attenuated vaccine strain (VZV-Oka). Structural analyses performed with the three glycosidases endo-beta-N-acetylglucosaminidase H (endoglycosidase H), endo-beta-N-acetylglucosaminidase F (endoglycosidase F), and endo-alpha-N-acetylgalactosaminidase demonstrated that gp118 was predominantly an N-linked complex type glycoprotein built upon a polypeptide backbone of approximately 79,000 Da. Sialic acid residues were present on the mature glycoprotein, but these terminal sugars were absent from the partially glycosylated intermediate forms recovered from monensin-treated infected cultures. Unlike another VZV-specified glycoprotein gp98, no new oligosaccharide moieties were observed on gp118 after addition of tunicamycin to VZV-infected cultures. By plaque reduction assays with a panel of monoclonal antibodies, we defined an epitope on this glycoprotein which elicited a complement-independent neutralizing antibody response of high magnitude. The epitope was highly conserved, since it was present on a laboratory VZV strain, wild type isolates, as well as the attenuated vaccine strain (VZV-Oka). Competitive blocking experiments with the same anti-gp118 monoclonal antibodies indicated that four neutralizing antibodies were directed against similar or identical epitopes whereas one nonneutralizing antibody reacted with a different antigenic site. Thus, this study demonstrates the presence of an immunodominant neutralization epitope on native viral glycoprotein gp118. Under a new consensus nomenclature, this glycoprotein will be designated VZV gpIII.
水痘带状疱疹病毒（VZV）可产生多种糖蛋白，包括一种118,000道尔顿的成熟结构产物（gp118）。在制备针对低传代实验室毒株（VZV - 32）和减毒疫苗毒株（VZV - Oka）的鼠单克隆抗体后，对gp118的生物学和生化特性进行了研究。用三种糖苷酶，即内切β - N - 乙酰葡糖胺糖苷酶H（内切糖苷酶H）、内切β - N - 乙酰葡糖胺糖苷酶F（内切糖苷酶F）和内切α - N - 乙酰半乳糖胺糖苷酶进行的结构分析表明，gp118主要是一种N - 连接的复合型糖蛋白，其多肽主链约为79,000道尔顿。成熟糖蛋白上存在唾液酸残基，但从莫能菌素处理的感染培养物中回收的部分糖基化中间形式中没有这些末端糖。与另一种VZV产生的糖蛋白gp98不同，在VZV感染的培养物中添加衣霉素后，gp118上未观察到新的寡糖部分。通过用一组单克隆抗体进行蚀斑减少试验，我们确定了该糖蛋白上的一个表位，它可引发高强度的不依赖补体的中和抗体反应。该表位高度保守，因为它存在于实验室VZV毒株、野生型分离株以及减毒疫苗毒株（VZV - Oka）上。用相同的抗gp118单克隆抗体进行的竞争性阻断实验表明，四种中和抗体针对相似或相同的表位，而一种非中和抗体与不同的抗原位点反应。因此，本研究证明了天然病毒糖蛋白gp118上存在一个免疫显性中和表位。根据新的共识命名法，该糖蛋白将被命名为VZV gpIII。
