Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia.
Emerg Microbes Infect. 2020 Mar 17;9(1):601-604. doi: 10.1080/22221751.2020.1739565. eCollection 2020.
The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation, which is involved in host cell adhesion. We also predict the unique N- and O-linked glycosylation sites of spike glycoprotein that distinguish it from the SARS and underlines shielding and camouflage of COVID-19 from the host the defence system. Furthermore, our study also highlights the key finding that the S1 domain of COVID-19 spike glycoprotein potentially interacts with the human CD26, a key immunoregulatory factor for hijacking and virulence. These findings accentuate the unique features of COVID-19 and assist in the development of new therapeutics.
中国近期爆发的 COVID-19 病毒性肺炎是一个紧迫的全球公共卫生问题，其病死率和发病率均有所上升。在这里，我们报告了 COVID-19 刺突糖蛋白三聚体的模型结构，包括其在封闭（无配体）和开放（配体结合）构象下的结构，该蛋白参与宿主细胞的黏附。我们还预测了刺突糖蛋白特有的 N 连接和 O 连接糖基化位点，这些位点将 COVID-19 与 SARS 区分开来，并强调了 COVID-19 对宿主防御系统的屏蔽和伪装。此外，我们的研究还强调了一个关键发现，即 COVID-19 刺突糖蛋白的 S1 结构域可能与人类 CD26 相互作用，CD26 是一种关键的免疫调节因子，可劫持和增强病毒的毒力。这些发现突出了 COVID-19 的独特特征，并有助于开发新的治疗方法。
