The University of Texas at San Antonio (UTSA), Department of Chemistry, San Antonio, TX, 78249-0698, USA.
Protein J. 2021 Jun;40(3):260-295. doi: 10.1007/s10930-021-09967-8. Epub 2021 Feb 24.
The global pandemic that shut down the world in 2020 was caused by the virus, SARS CoV-2. The chemistry of the various nonstructural proteins (NSP3, NSP5, NSP12, NSP13, NSP14, NSP15, NSP16) of SARS CoV-2 is discussed. Secondly, a recent major focus of this pandemic is the variant strains of SARS CoV-2 that are increasingly occurring and more transmissible. One strain, called "D614G", possesses a glycine (G) instead of an aspartate (D) at position 614 of the spike protein. Additionally, other emerging strains called "501Y.V1" and "501Y.V2" have several differences in the receptor binding domain of the spike protein (N501Y) as well as other locations. These structural changes may enhance the interaction between the spike protein and the ACE2 receptor of the host, increasing infectivity. The global pandemic caused by SARS CoV-2 is a rapidly evolving situation, emphasizing the importance of continuing the efforts to interrogate and understand this virus.
2020 年导致全球停摆的大流行病毒是 SARS-CoV-2。本文讨论了 SARS-CoV-2 的各种非结构蛋白(NSP3、NSP5、NSP12、NSP13、NSP14、NSP15、NSP16)的化学性质。其次,该大流行最近的一个主要焦点是 SARS-CoV-2 的变异株越来越多地出现,并且更具传染性。一种名为“D614G”的菌株在其刺突蛋白的第 614 位上具有甘氨酸(G)而不是天冬氨酸(D)。此外,其他新兴的株,如“501Y.V1”和“501Y.V2”,在刺突蛋白的受体结合域(N501Y)以及其他位置存在几个差异。这些结构变化可能增强了刺突蛋白与宿主 ACE2 受体之间的相互作用,从而增加了感染性。由 SARS-CoV-2 引起的全球大流行是一个迅速演变的情况,强调了继续努力研究和了解这种病毒的重要性。