Alquraan Laiali, Alzoubi Karem H, Rababa'h Suzie Y
Department of Biology, Faculty of Science, Yarmouk University, Irbid, Jordan.
Department of Pharmacy Practice and Pharmacotherapeutics, College of Pharmacy, University of Sharjah, Sharjah, United Arab Emirates.
Inform Med Unlocked. 2023;39:101256. doi: 10.1016/j.imu.2023.101256. Epub 2023 Apr 25.
Numerous variations of the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), including D614G, B.1.1.7 (United Kingdom), B.1.1.28 (Brazil P1, P2), CAL.20C (Southern California), B.1.351 (South Africa), B.1.617 (B.1.617.1 Kappa & Delta B.1.617.2) and B.1.1.529, have been reported worldwide. The receptor-binding domain (RBD) of the spike (S) protein is involved in virus-cell binding, where virus-neutralizing antibodies (NAbs) react. Novel variants in the S-protein could maximize viral affinity for the human angiotensin-converting enzyme 2 (ACE2) receptor and increase virus transmission. Molecular detection with false-negative results may refer to mutations in the part of the virus's genome used for virus diagnosis. Furthermore, these changes in S-protein structure alter the neutralizing ability of NAbs, resulting in a reduction in vaccine efficiency. Further information is needed to evaluate how new mutations may affect vaccine efficacy.
已在全球范围内报告了严重急性呼吸综合征冠状病毒2(SARS-CoV-2)的多种变体,包括D614G、B.1.1.7(英国)、B.1.1.28(巴西P1、P2)、CAL.20C(南加利福尼亚)、B.1.351(南非)、B.1.617(B.1.617.1卡帕和德尔塔B.1.617.2)以及B.1.1.529。刺突(S)蛋白的受体结合域(RBD)参与病毒与细胞的结合,病毒中和抗体(NAb)在此处发生反应。S蛋白中的新型变体可能会使病毒对人血管紧张素转换酶2(ACE2)受体的亲和力最大化,并增加病毒传播。出现假阴性结果的分子检测可能与用于病毒诊断的病毒基因组部分发生的突变有关。此外,S蛋白结构的这些变化改变了NAb的中和能力,导致疫苗效率降低。需要更多信息来评估新突变可能如何影响疫苗效力。