论文标题
通过氨基酸残基的保守进化模式，具有ACE2结合SARS-COV和SARS-COV-2
Featuring ACE2 binding SARS-CoV and SARS-CoV-2 through a conserved evolutionary pattern of amino acid residues
论文作者
论文摘要
尖峰（S）糖蛋白介导冠状病毒进入宿主细胞。 S蛋白的S1亚基包含能够识别不同宿主受体的受体结合结构域（RBD），突出了其显着的能力，可以适应沿病毒进化的宿主。虽然峰值蛋白中的RBD是病毒受体相互作用的决定因素，但活性残基位于受体结合基序（RBM），RBD中的一个区域在RBD中起着与受体外表面结合的基本作用。在这里，我们解决了以下假设：SARS-COV和SARS-COV-2菌株能够使用血管紧张素转换酶2（ACE2）蛋白已沿病毒演化调整其RBM，以探索由残基YGF驱动的特定构象拓扑，以感染宿主细胞。我们还推测，这种基于YGF的机制可以充当RBM上的蛋白质特征，以区分能够使用ACE2作为细胞进入受体的冠状病毒。
Spike (S) glycoproteins mediate the coronavirus entry into the host cell. The S1 subunit of S-proteins contains the receptor-binding domain (RBD) that is able to recognize different host receptors, highlighting its remarkable capacity to adapt to their hosts along the viral evolution. While RBD in spike proteins is determinant for the virus-receptor interaction, the active residues lie at the receptor-binding motif (RBM), a region located in RBD that plays a fundamental role binding the outer surface of their receptors. Here, we address the hypothesis that SARS-CoV and SARS-CoV-2 strains able to use angiotensin-converting enzyme 2 (ACE2) proteins have adapted their RBM along the viral evolution to explore specific conformational topology driven by the residues YGF to infect host cells. We also speculate that this YGF-based mechanism can act as a protein signature located at the RBM to distinguish coronaviruses able to use ACE2 as a cell entry receptor.
