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首页> 外文期刊>Journal of Virology >Characterization of a herpes simplex virus type 2 75,000-molecular-weight glycoprotein antigenically related to herpes simplex virus type 1 glycoprotein C.
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Characterization of a herpes simplex virus type 2 75,000-molecular-weight glycoprotein antigenically related to herpes simplex virus type 1 glycoprotein C.

机译：疱疹病毒275,000分子量糖蛋白的疱疹病毒的表征抗原与单纯疱疹病毒1型糖蛋白C.

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Evidence is presented that the herpes simplex virus type 2 glycoprotein previously designated gF is antigenically related to herpes simplex virus type 1 gC (gC-1). An antiserum prepared against type 1 virion envelope proteins immunoprecipitated gF of type 2 (gF-2), and competition experiments revealed that the anti-gC-1 component of the antiserum was responsible for the anti-gF-2 cross-reactivity. An antiserum prepared against fully denatured purified gF-2, however, and three anti-gF-2 monoclonal antibodies failed to precipitate any type 1 antigen, indicating that the extent of cross-reactivity between gC-1 and gF-2 may be limited. Several aspects of gF-2 synthesis and processing were investigated. Use of the enzymes endo-beta-N-acetylglucosaminidase H and alpha-D-N-acetylgalactosaminyl oligosaccharidase revealed that the fully processed form of gF-2 (about 75,000 [75K] apparent molecular weight) had both complex-type N-linked and O-linked oligosaccharides, whereas newly synthesized forms (67K and 69K) had only high-mannose N-linked oligosaccharides. These last two forms were both reduced in size to 54K by treatment with endo-beta-N-acetylglucosaminidase H and therefore appear to differ only in the number of N-linked chains. Neutralization tests and radioiodination experiments revealed that gF-2 is exposed on the surfaces of virions and that the 75K form of gF-2 is exposed on cell surfaces. The similarities and differences of gF-2 and gC-1 are discussed in light of recent mapping results which suggest collinearity of their respective genes.
机译：提出了证据表明单纯疱疹病毒2型糖蛋白先前指定的GF与单纯疱疹病毒1GC（GC-1）抗原有关。针对1型病毒藻包络蛋白的抗血清免疫沉淀的2型（GF-2）和竞争实验表明，抗血清的抗GC-1组分负责抗GF-2交叉反应性。然而，与完全变性纯化的GF-2制备的抗血清，并且三种抗GF-2单克隆抗体未被沉淀出任何类型的抗原，表明GC-1和GF-2之间的交叉反应程度可以受到限制。研究了GF-2合成和加工的几个方面。使用酶Endo-β-n-乙酰氨基氨基氨基氨基氨基酶H和α-DN-乙酰甘氨酸氨基苯基寡糖酶揭示了GF-2的完全加工形式（约75,000 [75K]表观分子量）均具有复杂的N-连接和O-连接的寡糖，而新合成的形式（67K和69K）只有高甘露糖N-连接的低聚糖。通过用endo-β-n-乙酰葡糖胺氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基氨基酶H尺寸尺寸减小至54K，因此仅在N键链链的数量中似乎不同。中和试验和放射性学实验表明，GF-2暴露在病毒粒表面上，并且将75K形式的GF-2暴露在细胞表面上。根据最近的映射结果讨论了GF-2和GC-1的相似性和差异，这表明其各自基因的共同性。

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