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Structural and functional impact by SARS-CoV-2 Omicron spike mutations.
Zhang, Jun; Cai, Yongfei; Lavine, Christy L; Peng, Hanqin; Zhu, Haisun; Anand, Krishna; Tong, Pei; Gautam, Avneesh; Mayer, Megan L; Rits-Volloch, Sophia; Wang, Shaowei; Sliz, Piotr; Wesemann, Duane R; Yang, Wei; Seaman, Michael S; Lu, Jianming; Xiao, Tianshu; Chen, Bing.
  • Zhang J; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Cai Y; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Lavine CL; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
  • Peng H; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Zhu H; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Anand K; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Tong P; 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, Cambridge, MA 02139, USA.
  • Gautam A; 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, Cambridge, MA 02139, USA.
  • Mayer ML; The Harvard Cryo-EM Center for Structural Biology, 250 Longwood Avenue, Boston, MA 02115, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
  • Rits-Volloch S; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA.
  • Wang S; Codex BioSolutions, Inc., 12358 Parklawn Drive, Rockville, MD 20852, USA.
  • Sliz P; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
  • Wesemann DR; 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, Cambridge, MA 02139, USA.
  • Yang W; Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.
  • Seaman MS; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
  • Lu J; Codex BioSolutions, Inc., 12358 Parklawn Drive, Rockville, MD 20852, USA; Department of Biochemistry and Molecular and Cellular Biology, Georgetown University School of Medicine, 3900 Reservoir Road NW, Washington, DC 20057, USA.
  • Xiao T; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA. Electronic address: xiao@crystal.harvard.edu.
  • Chen B; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA. Electronic address: bchen@crystal.harvard.edu.
Cell Rep ; 39(4): 110729, 2022 04 26.
Article in English | MEDLINE | ID: covidwho-1783229
ABSTRACT
The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutralizing antibodies. These results suggest that Omicron S has acquired an extraordinary ability to evade host immunity by excessive mutations, which also compromise its fusogenic capability.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Type of study: Experimental Studies Topics: Variants Limits: Humans Language: English Journal: Cell Rep Year: 2022 Document Type: Article Affiliation country: J.celrep.2022.110729

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Type of study: Experimental Studies Topics: Variants Limits: Humans Language: English Journal: Cell Rep Year: 2022 Document Type: Article Affiliation country: J.celrep.2022.110729