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Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study.
- Source :
-
Science (New York, N.Y.) [Science] 2021 Oct 22; Vol. 374 (6566), pp. 472-478. Date of Electronic Publication: 2021 Sep 23. - Publication Year :
- 2021
-
Abstract
- Antibody-based therapeutics and vaccines are essential to combat COVID-19 morbidity and mortality after severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Multiple mutations in SARS-CoV-2 that could impair antibody defenses propagated in human-to-human transmission and spillover or spillback events between humans and animals. To develop prevention and therapeutic strategies, we formed an international consortium to map the epitope landscape on the SARS-CoV-2 spike protein, defining and structurally illustrating seven receptor binding domain (RBD)–directed antibody communities with distinct footprints and competition profiles. Pseudovirion-based neutralization assays reveal spike mutations, individually and clustered together in variants, that affect antibody function among the communities. Key classes of RBD-targeted antibodies maintain neutralization activity against these emerging SARS-CoV-2 variants. These results provide a framework for selecting antibody treatment cocktails and understanding how viral variants might affect antibody therapeutic efficacy.
- Subjects :
- Antibodies, Neutralizing therapeutic use
Antibodies, Viral therapeutic use
Antigens, Viral chemistry
Antigens, Viral immunology
COVID-19 therapy
Humans
Immunodominant Epitopes chemistry
Protein Binding
Protein Domains
Spike Glycoprotein, Coronavirus chemistry
Antibodies, Neutralizing immunology
Antibodies, Viral immunology
Epitope Mapping
Immunodominant Epitopes immunology
SARS-CoV-2 immunology
Spike Glycoprotein, Coronavirus immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 374
- Issue :
- 6566
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 34554826
- Full Text :
- https://doi.org/10.1126/science.abh2315