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首页> 外文期刊>AIDS Research and Human Retroviruses >Antiviral Activity of the Interferon-Induced Cellular Protein BST-2/Tetherin
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Antiviral Activity of the Interferon-Induced Cellular Protein BST-2/Tetherin

机译：干扰素诱导的细胞蛋白BST-2 / Tetherin的抗病毒活性。

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摘要

Pathogenic microorganisms encode proteins that antagonize specific aspects of innate or adaptive immunity. Just as the study of the HIV-1 accessory protein Vif led to the identification of cellular cytidine deaminases as host defense proteins, the study of HIV-1 Vpu recently led to the discovery of the interferon-induced transmembrane protein BST-2 (CD317; tetherin) as a novel component of the innate defense against enveloped viruses. BST-2 is an unusually structured protein that restricts the release of fully formed progeny virions from infected cells, presumably by a direct retention mechanism that is independent of any viral protein target. Its spectrum of activity includes at least four virus families: retroviruses, filoviruses, arenaviruses, and herpesviruses. Viral antagonists of BST-2 include HIV-1 Vpu, HIV-2 and SIV Env, SIV Nef, the Ebola envelope glycoprotein, and the K5 protein of KSHV. The mechanisms of antagonism are diverse and currently include viral cooption of cellular endosomal trafficking and protein degradation pathways, including those mediated by ubiquitination. Orthologs of human BST-2 are present in mammals. Primate BST-2 proteins are differentially sensitive to antagonism by lentiviral Vpu and Nef proteins, suggesting that BST-2 has subjected lentiviruses to evolutionary pressure and presents barriers to cross-species transmission. BST-2 functions not only as an effector of the interferon-induced antiviral response but also as a negative feedback regulator of interferon production by plasmacytoid dendritic cells. Future work will focus on the role and regulation of BST-2 during the innate response to viral infection, on the mechanisms of restriction and of antagonism by viral gene products, and on the role of BST-2 in primate lentiviral evolution. The augmentation of BST-2 activity and the inhibition of virally encoded antagonists, in particular Vpu, represent new approaches to the prevention and treatment of HIV-1 infection.
机译：病原微生物编码的蛋白质可拮抗先天或适应性免疫的特定方面。正如对HIV-1辅助蛋白Vif的研究导致将细胞胞苷脱氨酶鉴定为宿主防御蛋白一样，对HIV-1 Vpu的研究最近也导致了干扰素诱导的跨膜蛋白BST-2的发现（CD317; tetherin）作为先天防御包膜病毒的新成分。 BST-2是一种异常结构化的蛋白质，它可能通过直接保留机制来限制感染的细胞中完全形成的子代病毒体的释放，而这种直接保留机制与任何病毒蛋白靶标无关。它的活动范围包括至少四个病毒家族：逆转录病毒，丝状病毒，沙粒病毒和疱疹病毒。 BST-2的病毒拮抗剂包括HIV-1 Vpu，HIV-2和SIV Env，SIV Nef，埃博拉病毒包膜糖蛋白和KSHV的K5蛋白。拮抗作用的机制是多种多样的，目前包括细胞内体运输和蛋白质降解途径（包括由泛素介导的那些途径）的病毒共存选择。人BST-2的直系同源物存在于哺乳动物中。灵长类动物BST-2蛋白对慢病毒Vpu和Nef蛋白的拮抗作用有不同的敏感性，表明BST-2使慢病毒受到进化压力并为跨物种传播提供了障碍。 BST-2不仅充当干扰素诱导的抗病毒反应的效应子，而且还充当浆细胞样树突状细胞产生干扰素的负反馈调节剂。未来的工作将侧重于BST-2在对病毒感染的先天反应过程中的作用和调节，病毒基因产物的限制和拮抗作用机制以及BST-2在灵长类慢病毒进化中的作用。 BST-2活性的增强和病毒编码拮抗剂尤其是Vpu的抑制代表了预防和治疗HIV-1感染的新方法。

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  • 来源
    《AIDS Research and Human Retroviruses》 |2009年第12期|1197-1210|共14页
  • 作者

    Andrey Tokarev; Mark Skasko; Kathleen Fitzpatrick; John Guatelli;

  • 作者单位

    Department of Medicine, University of California San Diego, and the San Diego Veterans Affairs Healthcare System, La Jolla, California 92093-0679.;

    Department of Medicine, University of California San Diego, and the San Diego Veterans Affairs Healthcare System, La Jolla, California 92093-0679.;

    Department of Medicine, University of California San Diego, and the San Diego Veterans Affairs Healthcare System, La Jolla, California 92093-0679.;

    Department of Medicine, University of California San Diego, and the San Diego Veterans Affairs Healthcare System, La Jolla, California 92093-0679.;

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