美国华盛顿大学David Veesler研究团队揭示SARS-CoV-2刺突蛋白的结构、功能和抗原性。这一研究成果于2020年3月9日发表在《细胞》杂志上。

他们表示SARS-CoV-2 S利用ACE2进入细胞，并且SARS-CoV-2 S和SARS-CoV S的受体结合域与人ACE2的亲和力相似，与人体SARS-CoV-2的有效传播相关。他们发现，SARS-CoV-2 S糖蛋白在S1 / S2亚基之间的边界处具有furin蛋白酶切割位点，该位点在生物发生过程中被加工，并将这种病毒与SARS-CoV和SARS相关的CoV分开。他们确定了SARS-CoV-2 S胞外域三聚体的冷冻电镜结构，为疫苗和病毒侵入抑制剂的设计提供了蓝图。最后，他们证明了SARS-CoV S鼠多克隆抗体有效地抑制了SARS-CoV-2 S介导的细胞侵入，这表明接种疫苗后，交叉中和抗体可以被诱导靶向保守S抗原决定簇。

研究人员表示，SARS-CoV-2的出现导致了超过90000感染和超过3000人死亡。新冠病毒表面刺突(S)糖蛋白能够促进细胞侵入，并且是主要的抗体靶标。

附：英文原文

Title: Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Author: Alexandra C. Walls, Young-Jun Park, M. Alejandra Tortorici, Abigail Wall, Andrew T. McGuire, David Veesler

Issue&Volume: 2020-03-09

Abstract: The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.

DOI: 10.1016/j.cell.2020.02.058

Source: https://www.cell.com/cell/fulltext/S0092-8674(20)30262-2