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用不同抗血清和人脑脊液对1型单纯疱疹病毒抗原进行免疫沉淀

Immunoprecipitation of herpes simplex virus type 1 antigens with different antisera and human cerebrospinal fluids.

作者信息

Pauli G, Ludwig H

出版信息

Arch Virol. 1977;53(1-2):139-55. doi: 10.1007/BF01314855.

DOI:10.1007/BF01314855
PMID:192180
Abstract

Rabbit convalescent and hyperimmune sera, human patient and blood donor sera, as well as cerebrospinal fluids of humans with herpes simplex virus encephalitis all recognize similar major antigenic components in herpes simplex virus infected rabbit or human cells as shown by electrophoretic analysis of immunoprecipitates. Besides the main glycoproteins with an apparent molecular weight of 100,000 (peak I) the antisera precipitate glycoproteins in a region of an apparent mol. wt. of 60,000--80,000 (peak II), which were resolved into distinct glycoprotein species only by antibody-containing cerebrospinal fluids. The peak II glycoproteins appear on the surface of the infected cell early, and absorb neutralizing antibodies, whereas the peak I glycoproteins are less accessible. Both antigens can be demonstrated in the cell as early as about 2 hours post infection. All major antigenic components studied were found to be glycosylated except one protein with an apparent mol. wt. of 110,000. The herpesvirus specificity of these antigens is demonstrated by a variety of control experiments. The antigens detected are virion components.

摘要

兔恢复期血清和超免疫血清、人类患者血清和献血者血清,以及单纯疱疹病毒性脑炎患者的脑脊液,通过对免疫沉淀物的电泳分析表明,它们在感染单纯疱疹病毒的兔或人类细胞中都能识别相似的主要抗原成分。除了表观分子量为100,000的主要糖蛋白(峰I)外,抗血清还能沉淀表观分子量在60,000 - 80,000区域的糖蛋白(峰II),只有含抗体的脑脊液才能将其分解为不同的糖蛋白种类。峰II糖蛋白早期出现在感染细胞表面,并能吸收中和抗体,而峰I糖蛋白较难接近。两种抗原在感染后约2小时即可在细胞中检测到。除了一种表观分子量为110,000的蛋白质外,所有研究的主要抗原成分都被发现是糖基化的。这些抗原的疱疹病毒特异性通过各种对照实验得到证实。检测到的抗原是病毒粒子成分。

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Evidence for a Gp85-related glycoprotein in cells transformed by the Bryan high titer strain of Rous sarcoma virus.劳氏肉瘤病毒布莱恩高滴度毒株转化的细胞中存在与Gp85相关糖蛋白的证据。
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