Strebel K, Klimkait T, Martin M A
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.
Science. 1988 Sep 2;241(4870):1221-3. doi: 10.1126/science.3261888.
A 16-kilodalton protein expressed in cells producing the human immunodeficiency virus (HIV-1) was identified as the gene product of the vpu open reading frame. When expressed in vitro, the 81-amino acid vpu protein reacted with about one-third of the serum samples from AIDS patients that were tested, indicating that the vpu open reading frame is expressed in vivo as well. Introduction of a frame-shift mutation into the vpu open reading frame did not significantly interfere with expression of the major viral proteins in a transient expression system. However, a five- to tenfold reduction in progeny virions was observed after the infection of T lymphocytes with the mutant virus. These data suggest that the vpu gene product is required for efficient virus replication and may have a role in assembly or maturation of progeny virions.
在产生人类免疫缺陷病毒（HIV-1）的细胞中表达的一种16千道尔顿的蛋白质被鉴定为vpu开放阅读框的基因产物。当在体外表达时，81个氨基酸的vpu蛋白与所检测的约三分之一艾滋病患者的血清样本发生反应，这表明vpu开放阅读框在体内也有表达。将移码突变引入vpu开放阅读框在瞬时表达系统中并未显著干扰主要病毒蛋白的表达。然而，在用突变病毒感染T淋巴细胞后，观察到子代病毒颗粒减少了五到十倍。这些数据表明，vpu基因产物是有效病毒复制所必需的，并且可能在子代病毒颗粒的组装或成熟中发挥作用。
