SARS-CoV-2表面凸起糖蛋白的結構、功能和抗原性

SARS-CoV-2表面凸起糖蛋白的結構、功能和抗原性

作者：

小柯機器人

發布時間：2020/3/18 15:32:28

美國華盛頓大學David Veesler研究團隊揭示SARS-CoV-2刺突蛋白的結構、功能和抗原性。這一研究成果於2020年3月9日發表在《細胞》雜誌上。

他們表示SARS-CoV-2 S利用ACE2進入細胞，並且SARS-CoV-2 S和SARS-CoV S的受體結合域與人ACE2的親和力相似，與人體SARS-CoV-2的有效傳播相關。他們發現，SARS-CoV-2 S糖蛋白在S1 / S2亞基之間的邊界處具有furin蛋白酶切割位點，該位點在生物發生過程中被加工，並將這種病毒與SARS-CoV和SARS相關的CoV分開。他們確定了SARS-CoV-2 S胞外域三聚體的冷凍電鏡結構，為疫苗和病毒侵入抑制劑的設計提供了藍圖。最後，他們證明了SARS-CoV S鼠多克隆抗體有效地抑制了SARS-CoV-2 S介導的細胞侵入，這表明接種疫苗後，交叉中和抗體可以被誘導靶向保守S抗原決定簇。

研究人員表示，SARS-CoV-2的出現導致了超過90000感染和超過3000人死亡。新冠病毒表面刺突(S)糖蛋白能夠促進細胞侵入，並且是主要的抗體靶標。

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

Cell：《細胞》，創刊於1974年。隸屬於細胞出版社，最新IF：36.216