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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural insight into HIV-1 capsid recognition by rhesus TRIM5α
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Structural insight into HIV-1 capsid recognition by rhesus TRIM5α

机译：恒河猴TRIM5α对HIV-1衣壳识别的结构见解

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摘要

Tripartite motif protein isoform 5 alpha (TRIM5α) is a potent antiviral protein that restricts infection by HIV-1 and other retrovi-ruses. TRIM5α recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner. Upon binding, TRIM5α induces premature disassembly of the viral capsid and activates the downstream innate immune response. We have determined the crystal structure of the rhesus TRIM5α PRY/ SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5α PRY/SPRY, but not the human TRIM5α PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5α that is capable of interacting with viral cap-sids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5α-mediated retroviral restriction.
机译：三方基序蛋白同工型5α（TRIM5α）是有效的抗病毒蛋白，可限制HIV-1和其他逆转录病毒的感染。 TRIM5α通过B30.2（PRY / SPRY）域以物种特异性方式识别逆转录病毒衣壳的晶格。结合后，TRIM5α诱导病毒衣壳过早分解，并激活下游先天免疫反应。我们已经确定了恒河猴TRIM5αPRY / SPRY域的晶体结构，揭示了衣壳结合的基本特征。冷冻电子显微镜和生化数据的综合显示，单体恒河猴TRIM5αPRY / SPRY，而不是人类TRIM5αPRY / SPRY，可以与HIV-1衣壳蛋白组件结合，而不会引起衣壳的破坏。这表明单独的PRY / SPRY结构域构成了TRIM5α的重要模式感测组件，该组件能够与不同曲率的病毒衣壳相互作用。我们的结果为TRIM5α介导的逆转录病毒限制机制提供了分子见解。

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    Haitao Yang; Xiaoyun Ji; Gongpu Zhao; Jiying Ning; Qi Zhao; Christopher Aiken; Angela M. Gronenborn; Peijun Zhang; Yong Xiong;

  • 作者单位

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;

    Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260;

    Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260;

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;

    Department of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232;

    Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260;

    Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260;

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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  • 正文语种 eng
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