论文标题
与SARS-COV和相关的SARS样冠状病毒相比
Structural modeling of 2019-novel coronavirus (nCoV) spike protein reveals a proteolytically-sensitive activation loop as a distinguishing feature compared to SARS-CoV and related SARS-like coronaviruses
论文作者
论文摘要
2019年的小说冠状病毒(2019-NCOV)目前正在引起广泛的爆发,集中在中国湖北省,这是一个主要的公共卫生问题。分类学上2019-NCOV与SARS-COV和与SARS相关的BAT冠状病毒密切相关,并且它似乎与SARS-COV共享一个常见的受体(ACE-2)。在这里,我们对2019-NCOV SPIKE糖蛋白进行结构建模。尽管受体结合模块中的氨基酸相似性相对较低,但我们的数据为2019-NCOV和SARS-COV之间的相似受体利用提供了支持。与SARS-COV相比,我们在受体结合(S1)和融合(S2)结构域的界面上确定了一个含有碱性氨基酸的扩展结构环,我们预计该域对蛋白水解敏感。我们建议这种循环更加与MERS-COV和其他冠状病毒相一致,并在2019-NCOV中存在这种结构环可能影响病毒稳定性和传播。
The 2019 novel coronavirus (2019-nCoV) is currently causing a widespread outbreak centered on Hubei province, China and is a major public health concern. Taxonomically 2019-nCoV is closely related to SARS-CoV and SARS-related bat coronaviruses, and it appears to share a common receptor with SARS-CoV (ACE-2). Here, we perform structural modeling of the 2019-nCoV spike glycoprotein. Our data provide support for the similar receptor utilization between 2019-nCoV and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV, we identify an extended structural loop containing basic amino acids at the interface of the receptor binding (S1) and fusion (S2) domains, which we predict to be proteolytically-sensitive. We suggest this loop confers fusion activation and entry properties more in line with MERS-CoV and other coronaviruses, and that the presence of this structural loop in 2019-nCoV may affect virus stability and transmission.