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Review Article

了解 SARS 病毒抑制剂的结构基础

卷 29, 期 4, 2022

发表于: 14 May, 2021

页: [666 - 681] 页: 16

弟呕挨: 10.2174/0929867328666210514122418

价格: $65

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摘要

2019 年 12 月在中国武汉市爆发的严重急性呼吸系统综合症 - 冠状病毒 (SARSCoV-2) 爆发并继续在国际上蔓延，构成了世界卫生组织宣布的大流行威胁，截至 2021 年 3 月 10 日，已确诊病例全球有 1.18 亿人死亡，260 万人死亡。在没有特定的抗病毒药物的情况下，对症治疗和身体隔离仍然是控制疾病和传染的选择。最近的抗病毒药物临床试验突出了一些有前景的化合物，如umifenovir（血凝素与SA介导的融合抑制剂只有70%的相似性）、remdesivir（RdRp核苷抑制剂）和favipiravir（RdRp抑制剂）。世卫组织针对几种有希望的类似物开展了一项多国临床试验，作为对抗 SARS 感染的潜在治疗方法。这种情况促使人们采用整体方法来发明安全和特定的药物，作为与 SARS 相关的病毒性疾病（包括 COVID-19）的预防和治疗方法。值得注意的是，世界各地的研究人员一直在尽最大努力应对危机，并产生了一个广泛而有前途的文献机构。它打开了一个范围，并允许在分子水平上了解病毒的进入。基于结构的方法可以揭示病毒进入相互作用的分子水平理解。参与氨基酸残基之间的配体谱和非共价相互作用是描述结构解释的关键信息。 SARS病毒进入宿主细胞的结构研究将揭示设计药物如进入抑制剂的可能策略。基于结构的方法展示了 3D 分子水平的细节。它显示了 SARS-CoV-2 刺突相互作用的特异性，它使用人血管紧张素转换酶 2（ACE2）作为受体进入，由人蛋白酶完成病毒融合和感染的过程。 3D 结构研究揭示了两个单元的存在，即 S1 和 S2。 S1被称为受体结合域（RBD），负责与宿主（ACE2）相互作用，S2单元参与病毒和细胞膜的融合。 TMPRSS2 介导 SARS CoV-2 的 S 蛋白中 S1/S2 亚基界面处的切割，导致病毒融合。与 S1 结合相关的构象差异会改变 ACE2 相互作用并抑制病毒融合。总体而言，详细的 3D 结构研究有助于了解病毒与宿主因子相互作用的 3D 结构基础，并为针对 SARS 相关病毒进入宿主细胞的新药发现过程开辟了空间。

关键词: 严重急性呼吸综合征 (SARS)、SARS-CoV2、COVID-19、受体结合域 (RBD)、蛋白质-蛋白质界面、进入抑制剂。

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