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.

中文翻译：

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SARS-CoV-2穗糖蛋白的结构，功能和抗原性。

SARS-CoV-2的出现导致了90,000例感染和3,000例死亡。冠状病毒刺突（S）糖蛋白促进进入细胞，是抗体的主要靶标。我们显示SARS-CoV-2 S使用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SARS-CoV的有效传播相关在人类中为-2。我们发现，SARS-CoV-2 S糖蛋白在S1 / S2亚基之间的边界处具有弗林蛋白酶切割位点，该位点在生物发生过程中被处理，并使该病毒与SARS-CoV和SARS相关的CoV分开。我们确定了SARS-CoV-2 Sectodomain三聚体的低温EM结构，为疫苗和病毒进入抑制剂的设计提供了蓝图。最后，