CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion.
CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion.
复制标题
通过蛋白水解消化确定的人类免疫缺陷病毒包膜糖蛋白 gp120 的 CD4 结合区。
DOI：
10.1073/pnas.88.24.11320
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发表时间：
1991
影响因子：
11.1
通讯作者：
Wiley,DC
中科院分区：
文献类型：
--
作者：
Pollard,SR;Meier,W;Chow,P;Rosa,JJ;Wiley,DC
人类免疫缺陷病毒1型gp120包膜糖蛋白与细胞表面蛋白CD4高亲和力结合。在这里，我们报告了使用蛋白分解来定义涉及CD4结合的gp120区域。在残基269位用金黄色葡萄球菌V8蛋白酶或在残基432位用胰酶切割gp120会破坏CD4结合。这些相同的部位受到结合的CD4的保护，使其不被蛋白质水解性切割。、第144、166、172和315位的裂解不影响结合，也不受结合的CD_4的保护，表明这些区域对结合CD_4不是关键的。在与CD4共沉淀物中发现的所有蛋白水解物片段都是通过二硫键共价结合的，并包含完整的gp120分子。Nygren等人之前的结论。访问数/每百万人：Reach for[Nygren，A.，Bergman，T.，Matthews，T.娜塔莉。阿卡德。SCI。美国85,6543-6546]大的和小的(95-kDa和25-kDa)V8蛋白水解性片段都独立地与CD4结合，通过他们的实验没有区别，这里发现的结果是小片段与CD4免疫沉淀，而二硫键连接到大片段。
The gp120 envelope glycoprotein of human immunodeficiency virus type 1 binds the cell surface protein CD4 with high affinity. Here we report the use of proteolysis to define regions of gp120 involved in CD4 binding. Cleavage of gp120 with Staphylococcus aureus V8 protease at residue 269 or with trypsin at residue 432 destroys CD4 binding. These same sites are protected from proteolytic cleavage by bound CD4. Cleavages at 64, 144, 166, 172, and 315 do not affect binding and are not protected by bound CD4, indicating that these regions are not critical for binding CD4. All proteolytic fragments found in coprecipitates with CD4 were covalently associated via disulfides and comprised complete gp120 molecules. Previous conclusions by Nygren et al. [Nygren, A., Bergman, T., Matthews, T., Jornvall, H. & Wigzell, H. (1988) Proc. Natl. Acad. Sci. USA 85, 6543-6546] that both large and small (95-kDa and 25-kDa) V8 proteolytic fragments bind CD4, independently, are not distinguished by their experiments from the result found here that the small fragment immunoprecipitates with CD4 while disulfide-linked to the larger fragment.