Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.

Autor: 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., 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., 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., Lavine CL; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA., Rawson S; SBGrid Consortium, Harvard Medical School, 250 Longwood Avenue, 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., 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 Immunology and Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA., Gautam A; 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 S; Codex BioSolutions, Inc., 401 Professional Drive, Gaithersburg, MD 20879, USA., Sterling SM; 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., Walsh RM Jr; 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., Rits-Volloch S; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA., Lu J; 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, NW, Washington, DC 20057, USA., Wesemann DR; 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., 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., Chen B; Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115, USA. bchen@crystal.harvard.edu.; Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
Jazyk: angličtina
Zdroj: Science (New York, N.Y.) [Science] 2021 Aug 06; Vol. 373 (6555), pp. 642-648. Date of Electronic Publication: 2021 Jun 24.
DOI: 10.1126/science.abi9745
Abstrakt: 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.
(Copyright © 2021, American Association for the Advancement of Science.)
Databáze: MEDLINE
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