Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Viruses. 2021 Oct 14;13(10):2069. doi: 10.3390/v13102069.
Human norovirus (HuNoV) infection is a global health and economic burden. Currently, there are no licensed HuNoV vaccines or antiviral drugs available. The protease encoded by the HuNoV genome plays a critical role in virus replication by cleaving the polyprotein and is an excellent target for developing small-molecule inhibitors. The current strategy for developing HuNoV protease inhibitors is by targeting the enzyme's active site and designing inhibitors that bind to the substrate-binding pockets located near the active site. However, subtle differential conformational flexibility in response to the different substrates in the polyprotein and structural differences in the active site and substrate-binding pockets across different genogroups, hamper the development of effective broad-spectrum inhibitors. A comparative analysis of the available HuNoV protease structures may provide valuable insight for identifying novel strategies for the design and development of such inhibitors. The goal of this review is to provide such analysis together with an overview of the current status of the design and development of HuNoV protease inhibitors.
人类诺如病毒(HuNoV)感染是全球范围内的健康和经济负担。目前,尚无获得许可的 HuNoV 疫苗或抗病毒药物。HuNoV 基因组编码的蛋白酶在病毒复制中起着关键作用,通过切割多蛋白,是开发小分子抑制剂的理想靶点。目前开发 HuNoV 蛋白酶抑制剂的策略是针对酶的活性位点,设计与位于活性位点附近的底物结合口袋结合的抑制剂。然而,多蛋白中不同底物的细微差异构象灵活性以及不同基因型中活性位点和底物结合口袋的结构差异,阻碍了有效广谱抑制剂的开发。对现有 HuNoV 蛋白酶结构的比较分析可能为确定设计和开发此类抑制剂的新策略提供有价值的见解。本综述的目的是提供这种分析,并概述 HuNoV 蛋白酶抑制剂的设计和开发现状。