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Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant.
Zhang, Jun; Xiao, Tianshu; Cai, Yongfei; Lavine, Christy L; Peng, Hanqin; Zhu, Haisun; Anand, Krishna; Tong, Pei; Gautam, Avneesh; Mayer, Megan L; Walsh, Richard M; Rits-Volloch, Sophia; Wesemann, Duane R; Yang, Wei; Seaman, Michael S; Lu, Jianming; Chen, Bing.
  • Zhang J; Division of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Xiao T; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Cai Y; Division of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Lavine CL; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Peng H; Division of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Zhu H; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Anand K; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA, 02215, USA.
  • Tong P; Division of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Gautam A; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Mayer ML; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Walsh RM; Division of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
  • Rits-Volloch S; Ragon Institute of MGH, MIT, and Harvard, Boston, MA 02115, USA.
  • Wesemann DR; Division of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
  • Yang W; Ragon Institute of MGH, MIT, and Harvard, Boston, MA 02115, USA.
  • Seaman MS; The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
  • Lu J; Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
  • Chen B; The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
Science ; 374(6573): 1353-1360, 2021 Dec 10.
Article in English | MEDLINE | ID: covidwho-1483980
ABSTRACT
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 as well as 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 angiotensin converting enzyme 2 (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 amino-terminal domain of the S protein but only makes produces changes in the receptor binding domain (RBD), making the RBD a better target for therapeutic antibodies.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Immune Evasion / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / Membrane Fusion Topics: Variants Limits: Humans Language: English Journal: Science Year: 2021 Document Type: Article Affiliation country: Science.abl9463

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Immune Evasion / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / Membrane Fusion Topics: Variants Limits: Humans Language: English Journal: Science Year: 2021 Document Type: Article Affiliation country: Science.abl9463