Peptides derived from HIV‐1 gp120 co‐receptor binding domain form amyloid fibrils and enhance HIV‐1 infection
Peptides derived from HIV‐1 gp120 co‐receptor binding domain form amyloid fibrils and enhance HIV‐1 infection
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DOI：
10.1016/j.febslet.2014.03.016
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发表时间：
2014-05
期刊：
影响因子：
3.5
通讯作者：
Suiyi Tan;Lin Li;Lu Lu-Lu;Chungen Pan;Hong Lu;Y. Oksov;Xiaojuan Tang;Shibo Jiang;Shuwen Liu
中科院分区：
文献类型：
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作者：
Suiyi Tan;Lin Li;Lu Lu-Lu;Chungen Pan;Hong Lu;Y. Oksov;Xiaojuan Tang;Shibo Jiang;Shuwen Liu
淀粉样纤维在HIV-1感染中起重要作用。我们发现来自HIV-1 gp 120共受体结合区的肽，被定义为增强肽（EPs），可以形成淀粉样纤维，并显着增强HIV-1感染。EPs与病毒结合，促进HIV-1与靶细胞的相互作用。抗逆转录病毒药物（ARVs）的抗病毒疗效在EP的存在下大大受损。表没食子儿茶素没食子酸酯（Epigallocatechin gallate，EGCG）既能抑制由EP组成的纤维的形成，又能对抗EP介导的HIV-1感染增强作用。我们的研究结果确定了病毒衍生的淀粉样纤维，具有潜在的生物化学应用。蛋白质相互作用的结构总结EP 1和EP 1通过荧光技术结合（查看相互作用）EP 2和EP 2通过荧光技术结合（查看相互作用）EP 3和EP 3通过荧光技术结合（查看互动）SEVI和SEVI通过荧光技术结合（查看相互作用）通过透射电子显微镜观察EP 1和EP 1结合（查看相互作用）通过透射电子显微镜观察EP 2和EP 2结合（查看相互作用）EP 3和EP 3通过透射电子显微镜结合（查看相互作用）SEVI和SEVI通过透射电子显微镜结合（查看相互作用）
Amyloid fibrils play important roles in HIV-1 infection. We found peptides derived from the HIV-1 gp120 co-receptor binding region, which are defined as enhancing peptides (EPs), could form amyloid fibrils and remarkably enhance HIV-1 infection. EPs bound to the virus and promoted the interaction between HIV-1 and target cells. The antiviral efficacy of antiretroviral drugs (ARVs) was substantially impaired in the presence of EPs. Epigallocatechin gallate (EGCG) could both inhibit the formation of fibrils composed of EPs and counteract the EP-mediated enhancement of HIV-1 infection. Our findings identify viral derived amyloid fibrils that hold potential for biochemical applications.Structured summary of protein interactionsEP1andEP1bind by fluorescence technology (View interaction)EP2andEP2bind by fluorescence technology (View interaction)EP3andEP3bind by fluorescence technology (View interaction)SEVIandSEVIbind by fluorescence technology (View interaction)EP1andEP1bind by transmission electron microscopy (View interaction)EP2andEP2bind by transmission electron microscopy (View interaction)EP3andEP3bind by transmission electron microscopy (View interaction)SEVIandSEVIbind by transmission electron microscopy (View interaction)