Bae Y, Kingsman S M, Kingsman A J
Department of Biochemistry, University of Oxford, United Kingdom.
J Virol. 1997 Mar;71(3):2092-9. doi: 10.1128/JVI.71.3.2092-2099.1997.
The envelope protein of Moloney murine leukemia virus (Mo-MLV) is a complex glycoprotein that mediates receptor binding and entry via fusion with cell membranes. By using a series of substitution mutations and truncations in the Mo-MLV external envelope surface protein gp70, we have identified regions important for these processes. Firstly, truncations of gp70 revealed that the minimal continuous receptor-binding region is amino acids 9 to 230, in broad agreement with other studies. Secondly, within this region there are two key basic amino acids, Arg-83 and Arg-95, that are essential for receptor binding and may interact with a negatively charged residue(s) or with the pi electrons of the aromatic ring on a hydrophobic residue(s) in the basic amino acid transporter protein that is the Mo-MLV ecotropic receptor. Finally, we showed that outside the minimal receptor-binding region at amino acids 2 to 8, there is a region that is essential for postbinding fusion events.
莫洛尼鼠白血病病毒（Mo-MLV）的包膜蛋白是一种复杂的糖蛋白，它通过与细胞膜融合介导受体结合和进入。通过在Mo-MLV外膜表面蛋白gp70中使用一系列替代突变和截短，我们确定了这些过程的重要区域。首先，gp70的截短表明最小的连续受体结合区域是氨基酸9至230，这与其他研究广泛一致。其次，在该区域内有两个关键的碱性氨基酸，即精氨酸-83和精氨酸-95，它们对于受体结合至关重要，并且可能与带负电荷的残基或与作为Mo-MLV嗜亲性受体的碱性氨基酸转运蛋白中疏水残基上芳香环的π电子相互作用。最后，我们表明在氨基酸2至8的最小受体结合区域之外，有一个区域对于结合后融合事件至关重要。
