Lu X, Yu H, Liu S H, Brodsky F M, Peterlin B M
Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco, 94143-0703, USA.
Immunity. 1998 May;8(5):647-56. doi: 10.1016/s1074-7613(00)80569-5.
CD4 is the primary receptor for the human immunodeficiency virus (HIV). Nef is an accessory protein of HIV that decreases the expression of CD4 on the surface of infected cells. In this study, we identified the Nef binding protein 1 (NBP1), which interacts specifically with Nef in vitro and in vivo. Since it shares sequence similarity with the catalytic subunit of the vacuolar ATPase (V-ATPase) and complements the loss of this VMA13 gene in yeast, NBP1 is the human homolog of Vma13p. Direct interactions between Nef and NBP1 were correlated with the ability of Nef to internalize CD4. The expression of the antisense NBP1 abrogated these effects. We conclude that NBP1 helps to connect Nef with the endocytic pathway.
CD4是人类免疫缺陷病毒（HIV）的主要受体。Nef是HIV的一种辅助蛋白，它会降低受感染细胞表面CD4的表达。在本研究中，我们鉴定出了Nef结合蛋白1（NBP1），它在体外和体内均能与Nef特异性相互作用。由于它与液泡ATP酶（V-ATP酶）的催化亚基具有序列相似性，并且能弥补酵母中该VMA13基因的缺失，所以NBP1是Vma13p的人类同源物。Nef与NBP1之间的直接相互作用与Nef使CD4内化的能力相关。反义NBP1的表达消除了这些效应。我们得出结论，NBP1有助于将Nef与内吞途径联系起来。
