Snapshot of the interaction between HIV envelope glycoprotein 120 and protein disulfide isomerase.
Snapshot of the interaction between HIV envelope glycoprotein 120 and protein disulfide isomerase.
复制标题
HIV 包膜糖蛋白 120 和蛋白质二硫键异构酶之间相互作用的快照。
DOI：
10.1093/abbs/gmq024
复制
发表时间：
2010
影响因子：
3.7
通讯作者：
C. Chi
中科院分区：
文献类型：
--
作者：
Zhi;Zhimin Zhou;Zhan;C. Chi
人类免疫缺陷病毒-1（HIV-1）包膜糖蛋白120（gp 120）与细胞表面受体结合并介导HIV进入。以往的研究表明，细胞表面蛋白质二硫键异构酶（PDI）可能与gp 120的二硫键相互作用，从而促进HIV-1的进入。在本研究中，使用动力学捕获方法来捕获gp 120和PDI之间的二硫键交联中间体。制备活性位点突变体PDI，其中活性位点的C末端半胱氨酸被丝氨酸取代。活性位点突变的PDIs能够在体外通过混合二硫键与gp 120共价交联。交联效率由CD 4蛋白（HIV-1的主要受体）增强，并由杆菌肽（PDI抑制剂）和催化失活的PDI抑制。本研究结果提示，细胞表面PDI可能在HIV进入体内过程中发挥作用。
The human immunodeficiency virus-1 (HIV-1) envelope glycoprotein 120 (gp120) binds to cell surface receptors and mediates HIV entry. Previous studies suggest the cell surface protein disulfide isomerase (PDI) might interact with disulfide bond(s) of gp120 and thus facilitate HIV-1 entry. In the present study, a kinetic trapping approach was used to capture the disulfide cross-linking intermediate between gp120 and PDI. Active site mutant PDIs were prepared in which the C-terminal cysteine at the active site was replaced by a serine. The active site mutant PDIs were able to covalently cross-link with gp120 through a mixed disulfide bond in vitro. The cross-linking efficiency was enhanced by CD4 protein (primary receptor of HIV-1) and was inhibited both by bacitracin (a PDI inhibitor) and by catalytically inactive PDI. The present results suggested the cell surface PDI might play a role in HIV entry in vivo.
DOI：
10.1073/pnas.91.10.4559
发表时间：
1994-05-10
影响因子：
11.1
作者：
RYSER, HJP;LEVY, EM;DISCIULLO, GJ
通讯作者：
DISCIULLO, GJ