Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant,Science

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Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant
Science ( IF 44.7 ) Pub Date : 2021-10-26 , DOI: 10.1126/science.abl9463
Jun Zhang _{1,

2} , Tianshu Xiao _{1,

2} , Yongfei Cai _{1,

2} , Christy L Lavine ₃ , Hanqin Peng ₁ , Haisun Zhu ₄ , Krishna Anand ₄ , Pei Tong _{5,

6} , Avneesh Gautam _{5,

6} , Megan L Mayer _{7,

8} , Richard M Walsh _{7,

8} , Sophia Rits-Volloch ₁ , Duane R Wesemann _{5,

6} , Wei Yang ₄ , Michael S Seaman ₃ , Jianming Lu _{9,

10} , Bing Chen _{1,

2}

Affiliation

Division of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA, 02215, USA.
Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
Division of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
Ragon Institute of MGH, MIT, and Harvard, Boston, MA 02115, USA.
The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Codex BioSolutions, Inc., 401 Professional Drive, Gaithersburg, MD 20879, USA.
Department of Biochemistry and Molecular and Cellular Biology, Georgetown University School of Medicine, 3900 Reservoir Road, N.W., Washington, D.C. 20057, USA.

The Delta variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has outcompeted previously prevalent variants and become a dominant strain worldwide. We report the structure, function, and antigenicity of its full-length spike (S) trimer and those of the Gamma and Kappa variants and compare their characteristics with the G614, Alpha, and Beta variants. Delta S can fuse membranes more efficiently at low levels of cellular receptor ACE2, and its pseudotyped viruses infect target cells substantially faster than the other five variants, possibly accounting for its heightened transmissibility. Each variant shows different rearrangement of the antigenic surface of the N-terminal domain of the S protein, but only causes local changes in the receptor-binding domain (RBD), making the RBD a better target for therapeutic antibodies.

中文翻译：

SARS-CoV-2 Delta 变体的刺突蛋白的膜融合和免疫逃避

严重急性呼吸综合征冠状病毒 2 (SARS-CoV-2) 的 Delta 变种已经击败了之前流行的变种，成为全球范围内的主导毒株。我们报告了其全长刺突 (S) 三聚体以及 Gamma 和 Kappa 变体的结构、功能和抗原性，并将它们的特征与 G614、Alpha 和 Beta 变体进行了比较。 Delta S 可以在细胞受体 ACE2 水平较低的情况下更有效地融合细胞膜，其假型病毒感染靶细胞的速度比其他五种变体快得多，这可能是其传播性较高的原因。每种变体都显示出 S 蛋白 N 端结构域抗原表面的不同重排，但仅引起受体结合结构域 (RBD) 的局部变化，使 RBD 成为治疗性抗体的更好靶点。

更新日期：2021-10-26

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