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Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Cai, Yongfei; Zhang, Jun; Xiao, Tianshu; Lavine, Christy L; Rawson, Shaun; Peng, Hanqin; Zhu, Haisun; Anand, Krishna; Tong, Pei; Gautam, Avneesh; Lu, Shen; Sterling, Sarah M; Walsh, Richard M; Rits-Volloch, Sophia; Lu, Jianming; Wesemann, Duane R; Yang, Wei; Seaman, Michael S; Chen, Bing.
  • Cai Y; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Zhang J; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Xiao T; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Lavine CL; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Rawson S; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Peng H; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Zhu H; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
  • Anand K; SBGrid Consortium, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
  • Tong P; The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
  • Gautam A; Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
  • Lu S; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Sterling SM; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Walsh RM; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Rits-Volloch S; Division of Allergy and Immunology and Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.
  • Lu J; Division of Allergy and Immunology and Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.
  • Wesemann DR; Codex BioSolutions, Inc., 401 Professional Drive, Gaithersburg, MD 20879, USA.
  • Yang W; The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
  • Seaman MS; 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 ; 373(6555): 642-648, 2021 08 06.
Article in English | MEDLINE | ID: covidwho-1282051
ABSTRACT
Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Immune Evasion / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Topics: Variants Limits: Humans Language: English Journal: Science Year: 2021 Document Type: Article Affiliation country: Science.abi9745

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Immune Evasion / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Topics: Variants Limits: Humans Language: English Journal: Science Year: 2021 Document Type: Article Affiliation country: Science.abi9745