美國加州理工學院的科學家宣布，他們繪製出了艾滋病病毒（HIV）一種殼膜蛋白的結構圖，這使人類在研發艾滋病疫苗的道路上邁出了重要一步。　研究成果刊登在3月31日在線發表於的英國《自然・結構和分子生物學》雜誌。　

　　這種蛋白名為“ｇｐ１２０”。由於“ｇｐ１２０”蛋白在艾滋病病毒入侵人體的機製中發揮著非常重要的作用，因此成為研發艾滋病疫苗的一個重要突破口。　　

　　參與這項研究的研究員迪斯金說，進一步了解這種蛋白的結構，會使研發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.