美国加州理工学院的科学家宣布，他们绘制出了艾滋病病毒（HIV）一种壳膜蛋白的结构图，这使人类在研发艾滋病疫苗的道路上迈出了重要一步。　研究成果刊登在3月31日在线发表于的英国《自然·结构和分子生物学》杂志。

这种蛋白名为“ｇｐ１２０”。由于“ｇｐ１２０”蛋白在艾滋病病毒入侵人体的机制中发挥着非常重要的作用，因此成为研发艾滋病疫苗的一个重要突破口。

参与这项研究的研究员迪斯金说，进一步了解这种蛋白的结构，会使研发艾滋病疫苗的步伐加快。

Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity

Abstract Strategies to combat HIV-1 require structural knowledge of envelope proteins from viruses in HIV-1 clade C, the most rapidly spreading subtype in the world. We present a crystal structure containing a clade C gp120 envelope. The structure, a complex between gp120, the host receptor CD4 and the CD4-induced antibody 21c, reveals that the 21c epitope involves contacts with gp120, a nonself antigen, and with CD4, an autoantigen. Binding studies using wild-type and mutant CD4 show that 21c Fab binds CD4 in the absence of gp120, and that binding of 21c to clade C and HIV-2 gp120s requires the crystallographically observed 21c-CD4 interaction. Additional binding data suggest a role for the gp120 V1V2 loop in creating a high-affinity, but slow-forming, epitope for 21c after CD4 binds. These results contribute to a molecular understanding of CD4-induced antibodies and provide the first visualization to our knowledge of a potentially autoreactive antibody Fab complexed with both self and nonself antigens.