Structural basis of a shared antibody response to SARS-CoV-2

Author:

Yuan Meng1ORCID,Liu Hejun1ORCID,Wu Nicholas C.1ORCID,Lee Chang-Chun D.1ORCID,Zhu Xueyong1ORCID,Zhao Fangzhu234ORCID,Huang Deli2ORCID,Yu Wenli1ORCID,Hua Yuanzi1,Tien Henry1ORCID,Rogers Thomas F.25ORCID,Landais Elise236ORCID,Sok Devin346ORCID,Jardine Joseph G.36ORCID,Burton Dennis R.2347ORCID,Wilson Ian A.1348ORCID

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

2. Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.

3. IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USA.

5. Division of Infectious Diseases, Department of Medicine, University of California, San Diego, La Jolla, CA 92037, USA.

6. IAVI, New York, NY 10004, USA.

7. Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology, and Harvard University, Cambridge, MA 02139, USA.

8. The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.

Abstract

A common theme in antibody responses In the fight against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), antibodies are a key tool, both as potential therapeutics and to guide vaccine development. Yuan et al. focused on finding shared antibody responses, in which multiple individuals develop antibodies against the same antigen using the same genetic elements and modes of recognition. The authors identified the immunoglobulin heavy-chain variable region 3-53 gene as the most frequently used among 294 antibodies that target the receptor-binding domain (RBD) of the viral spike protein. These antibodies have few somatic mutations, and crystal structures of two neutralizing antibodies bound to the RBD show that mostly germline-encoded residues are involved in binding. The minimal affinity maturation and high potency of these antibodies is promising for vaccine design. Science , this issue p. 1119

Funder

National Institutes of Health

Bill and Melinda Gates Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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