Coronavirus disease 2019 is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). We have used bioinformatics to investigate seventeen mutations in the spike protein of SARS-CoV-2, as this mediates infection of human cells and is the target of most vaccine strategies and antibody-based therapies. Two mutations, H146Y and S221W, were identified as being most pathogenic. Mutations at positions D614G, A829T, and P1263L might also have deleterious effects on protein function. We hypothesized that candidate small molecules may be repurposed to combat viral infection. We investigated changes in binding energies of the ligands and the mutant proteins by assessing molecular docking. For an understanding of cellular function and organization, protein–protein interactions are also critical. Protein–protein docking for naïve and mutated structures of SARS-CoV-2 S protein was evaluated for their binding energy with the angiotensin-converting enzyme 2 (ACE2). These interactions might limit the binding of the SARS-CoV-2 spike protein to the ACE2 receptor or may have a deleterious effect on protein function that may limit infection. These results may have important implications for the transmission of SARS-CoV-2, its pathogenesis, and the potential for drug repurposing and immune therapies.

2019 年冠状病毒病是由严重急性呼吸系统综合症冠状病毒 2 (SARS-CoV-2) 引起的。我们使用生物信息学研究了 SARS-CoV-2 刺突蛋白的 17 个突变，因为它介导了人类细胞的感染，并且是大多数疫苗策略和基于抗体的疗法的目标。两个突变，H146Y 和 S221W，被确定为最具致病性。D614G、A829T 和 P1263L 位置的突变也可能对蛋白质功能产生有害影响。我们假设候选小分子可能被重新用于对抗病毒感染。我们通过评估分子对接研究了配体和突变蛋白结合能的变化。为了了解细胞功能和组织，蛋白质-蛋白质相互作用也很重要。评估了 SARS-CoV-2 S 蛋白的初始结构和突变结构的蛋白质-蛋白质对接，以确定它们与血管紧张素转换酶 2 (ACE2) 的结合能。这些相互作用可能会限制 SARS-CoV-2 刺突蛋白与 ACE2 受体的结合，或者可能对可能限制感染的蛋白质功能产生有害影响。这些结果可能对 SARS-CoV-2 的传播、其发病机制以及药物再利用和免疫疗法的潜力具有重要意义。