Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants-Reference-Cited by-全球学者库

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

Published:2021-08-06 Issue:6555 Volume:373 Page:642-648
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Cai Yongfei¹²^ORCID,Zhang Jun¹²^ORCID,Xiao Tianshu¹²^ORCID,Lavine Christy L.³^ORCID,Rawson Shaun⁴⁵⁶^ORCID,Peng Hanqin¹^ORCID,Zhu Haisun⁷^ORCID,Anand Krishna⁷,Tong Pei⁸^ORCID,Gautam Avneesh⁸^ORCID,Lu Shen⁹,Sterling Sarah M.⁵⁶^ORCID,Walsh Richard M.⁵⁶^ORCID,Rits-Volloch Sophia¹,Lu Jianming⁹¹⁰,Wesemann Duane R.⁸^ORCID,Yang Wei⁷^ORCID,Seaman Michael S.³^ORCID,Chen Bing¹²^ORCID

Affiliation:

1. Division of Molecular Medicine, Boston Children’s Hospital, 3 Blackfan Street, Boston, MA 02115, USA.

2. Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.

3. Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.

4. SBGrid Consortium, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.

5. The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.

6. Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

7. Institute for Protein Innovation, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA.

8. 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.

9. Codex BioSolutions, Inc., 401 Professional Drive, Gaithersburg, MD 20879, USA.

10. Department of Biochemistry and Molecular and Cellular Biology, Georgetown University School of Medicine, 3900 Reservoir Road, NW, Washington, DC 20057, USA.

Abstract

SARS-CoV-2 from alpha to epsilon As battles to contain the COVID-19 pandemic continue, attention is focused on emerging variants of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus that have been deemed variants of concern because they are resistant to antibodies elicited by infection or vaccination or they increase transmissibility or disease severity. Three papers used functional and structural studies to explore how mutations in the viral spike protein affect its ability to infect host cells and to evade host immunity. Gobeil et al . looked at a variant spike protein involved in transmission between minks and humans, as well as the B1.1.7 (alpha), B.1.351 (beta), and P1 (gamma) spike variants; Cai et al . focused on the alpha and beta variants; and McCallum et al . discuss the properties of the spike protein from the B1.1.427/B.1.429 (epsilon) variant. Together, these papers show a balance among mutations that enhance stability, those that increase binding to the human receptor ACE2, and those that confer resistance to neutralizing antibodies. —VV

Funder

National Institutes of Health

Emergent Ventures

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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