Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

Article

关键词: IMMUNODEFICIENCY-VIRUS TYPE-1;    CRYSTAL-STRUCTURE;    TRANSMEMBRANE GLYCOPROTEIN;    VARIABLE REGIONS;    ATOMIC-STRUCTURE;    BINDING;    RESOLUTION;    FRAGMENT;    AIDS;    HEMAGGLUTININ;   

DOI  :  10.1038/31405

来源: SCIE

【 摘 要 】

The entry of human Immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor on the cell surface. These interactions initiate a fusion of the viral and cellular membranes. Although gp120 can elicit virus-neutralizing antibodies, HIV eludes the Immune system. We have solved the X-ray crystal structure at 2.5 Angstrom resolution of an HIV-1 gp120 core complexed with a two-domain fragment of human con and an antigen-binding fragment of a neutralizing antibody that blocks chemokine-receptor binding. The structure reveals a cavity-laden CD4-gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion. Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to Intervene.

【 授权许可】

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