The Delta Variant Mutations in the Receptor Binding Domain of SARS-CoV-2 Show Enhanced Electrostatic Interactions with the ACE2.
The Delta Variant Mutations in the Receptor Binding Domain of SARS-CoV-2 Show Enhanced Electrostatic Interactions with the ACE2.
复制标题
SARS-CoV-2受体结合区的Delta变异显示与ACE2的静电相互作用增强。
DOI：
10.1016/j.medidd.2021.100114
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发表时间：
2021-12-04
影响因子：
--
通讯作者：
Amin M
中科院分区：
文献类型：
--
作者：
Goher SS;Ali F;Amin M
SARS-CoV-2中受体结合域(RBD)的突变被证明增强了它的复制、传播性和与宿主细胞的结合。最近，印度报道了一种新的病毒株，它包括RBD基因的突变(T478K和L452R)，这可能会增加感染率。在这里，我们利用分子力学(MM)和蒙特卡罗(MC)采样，证明了SARS-CoV-2的双突变株诱导了ACE2-e37的构象变化，通过与SARS-CoV-2-R403形成盐桥增强了静电相互作用。此外，我们观察到双突变结构导致RBD-T500和ACE2-D355之间的盐桥静电相互作用发生了显著的变化。这种相互作用的价值与其在WT蛋白中的价值相比损失了70%以上。
Mutations in the receptor binding domain (RBD) in SARS-CoV-2 are shown to enhance its replication, transmissibility, and binding to host cells. Recently, a new strain is reported in India that includes a mutation (T478K, and L452R) in the RBD, that is possibly increasing the infection rate. Here, using Molecular Mechanics (MM) and Monte Carlo (MC) sampling, we show that the double mutant variant of SARS-CoV-2 induced conformational change in ACE2-E37, which enhanced the electrostatic interactions by the formation of a salt-bridge with SARS-CoV-2-R403. In addition, we observed that the double mutated structure induced a significant change in the salt-bridge electrostatic interaction between RBD-T500 and ACE2-D355. Where that this interaction lost more than 70% of its value compared to its value in WT protein.