与人类免疫缺陷病毒（HIV）颗粒和马传染性贫血病毒核心相关的拓扑异构酶I活性。

Topoisomerase I activity associated with human immunodeficiency virus (HIV) particles and equine infectious anemia virus core.

作者信息

Priel E, Showalter S D, Roberts M, Oroszlan S, Segal S, Aboud M, Blair D G

机构信息

Microbiology and Immunology Unit, Faculty of Health Sciences, Ben-Gurion University, Beer-Sheva, Israel.

出版信息

EMBO J. 1990 Dec;9(12):4167-72. doi: 10.1002/j.1460-2075.1990.tb07640.x.

In the present study, we found a topoisomerase I (topo I) activity in two strains of human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) particles. The topo I activity was located in the EIAV cores and differed from the cellular topo I in its ionic requirements and response to ATP, indicating that these were two distinct forms of this enzyme. Topo I activity was removed from the viral lysates and viral cores by anti-topo I antiserum. The only protein recognized by this antiserum was an 11.5 kd protein in HIV lysate and 11 kd in EIAV lysate. We showed that the 11 kd protein recognized by the anti-topo I antiserum is the EIAV p11 nucleocapsid protein. Furthermore, purified topo I protein blocked the binding of the antibodies to the p11 protein and vice versa, purified p11 protein blocked the binding of these antibodies to the cellular topo I. These results suggest that the EIAV p11 nucleocapsid protein and the cellular topo I share similar epitopes.

在本研究中，我们在两株1型人类免疫缺陷病毒（HIV-1）和马传染性贫血病毒（EIAV）颗粒中发现了拓扑异构酶I（topo I）活性。拓扑异构酶I活性位于EIAV核心内，其离子需求和对ATP的反应不同于细胞拓扑异构酶I，这表明这是该酶的两种不同形式。通过抗拓扑异构酶I抗血清从病毒裂解物和病毒核心中去除拓扑异构酶I活性。该抗血清识别的唯一蛋白质在HIV裂解物中为11.5 kd蛋白，在EIAV裂解物中为11 kd蛋白。我们发现抗拓扑异构酶I抗血清识别的11 kd蛋白是EIAV p11核衣壳蛋白。此外，纯化的拓扑异构酶I蛋白可阻断抗体与p11蛋白的结合，反之亦然，纯化的p11蛋白可阻断这些抗体与细胞拓扑异构酶I的结合。这些结果表明，EIAV p11核衣壳蛋白与细胞拓扑异构酶I具有相似的表位。