Einfeld D, Hunter E
Department of Microbiology, University of Alabama, Birmingham 35294.
Proc Natl Acad Sci U S A. 1988 Nov;85(22):8688-92. doi: 10.1073/pnas.85.22.8688.
The structure of the Rous sarcoma virus envelope glycoprotein complex was studied by sedimentation gradient centrifugation analyses of detergent-solubilized wild-type and mutant envelope (env) gene products. These studies show that the envelope glycoprotein forms an oligomer during biosynthesis, which is most likely a trimer, and that this is the form of the complex found in virions. Our results are consistent with oligomer formation and transport out of the endoplasmic reticulum being closely linked. From analyses of mutant envelope proteins we conclude that the extracellular domain of the glycoprotein is sufficient for oligomer formation but that the transmembrane domain is required to stabilize this complex. Additional experiments suggest that interactions between external domains of the membrane-spanning, gp37 polypeptides are those most important for the formation of trimers. The significance of these observations to retroviral replication and implications for antiviral drug development are discussed.
通过对去污剂溶解的野生型和突变包膜（env）基因产物进行沉降梯度离心分析，研究了劳氏肉瘤病毒包膜糖蛋白复合物的结构。这些研究表明，包膜糖蛋白在生物合成过程中形成寡聚体，很可能是三聚体，并且这是在病毒粒子中发现的复合物形式。我们的结果与寡聚体形成和从内质网输出密切相关。通过对突变包膜蛋白的分析，我们得出结论，糖蛋白的胞外结构域足以形成寡聚体，但跨膜结构域是稳定该复合物所必需的。额外的实验表明，跨膜的gp37多肽的外部结构域之间的相互作用对三聚体的形成最为重要。讨论了这些观察结果对逆转录病毒复制的意义以及对抗病毒药物开发的影响。
