The outbreak of COVID-19 across the world has posed unprecedented and global challenges on multiple fronts. Most of the vaccine and drug development has focused on the spike proteins and viral RNA-polymerases. Using the bioinformatics and structural modeling approach, we modeled the structure of the envelope (E)-protein of novel SARS-CoV-2. The E-protein of this virus shares sequence similarity with that of SARS- CoV-1, and is highly conserved in the N-terminal regions. Incidentally, compared to spike proteins, E proteins demonstrate lower disparity and mutability among the isolated sequences. Using homology modeling, we found that the most favorable structure could function as a gated proton channel. Combining pocket estimation and docking with water, we determined that GLU 8 and ASN 15 in the N-terminal region were in close proximity to form H-bonds. Additionally, two distinct core structures were visible, the hydrophobic core and the central core, which may regulate the opening/closing of the channel. We propose this as a mechanism of viral proton channeling activity which may play a critical role in viral infection. In addition, it provides a structural basis and additional avenues for LAV development and generating therapeutic interventions against the virus.

中文翻译：

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结构性洞察新型SARS CoV-2 E蛋白在病毒感染中的推定作用：LAV发展和治疗策略的潜在目标

全球范围内COVID-19的爆发给多个领域带来了前所未有的全球挑战。大多数疫苗和药物开发都集中在刺突蛋白和病毒RNA聚合酶上。使用生物信息学和结构建模方法，我们对新型SARS-CoV-2的包膜（E）-蛋白质的结构进行了建模。该病毒的E蛋白与SARS-CoV-1具有相似的序列，在N端区域高度保守。顺便提及，与刺突蛋白相比，E蛋白在分离的序列之间显示出较低的差异性和可变性。使用同源建模，我们发现最有利的结构可以充当门控质子通道。结合口袋估计和水对接，我们确定N末端区域中的GLU 8和ASN 15紧密相邻以形成H键。另外，可见两个截然不同的核心结构，疏水性核心和中央核心，它们可以调节通道的打开/关闭。我们提出这是病毒质子通道活动的一种机制，可能在病毒感染中发挥关键作用。此外，它为LAV的发展和产生针对该病毒的治疗干预措施提供了结构基础和其他途径。