Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
| Autor: | Nicholas C. Wu, Xueyong Zhu, Marit J. van Gils, Jakob Kreye, Chang-Chun D Lee, Linghang Peng, Hejun Liu, Meng Yuan, Abigail M. Jackson, Dennis R. Burton, Andrew B. Ward, Rogier W. Sanders, David Nemazee, S. Momsen Reincke, Harald Prüss, Ian A. Wilson, Deli Huang |
|---|---|
| Přispěvatelé: | Medical Microbiology and Infection Prevention, AII - Infectious diseases |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
virology [COVID-19]
medicine.disease_cause Antibodies Viral metabolism [Angiotensin-Converting Enzyme 2] genetics [Spike Glycoprotein Coronavirus] Neutralization Germline Epitopes genetics [Antigens Viral] immunology [SARS-CoV-2] immunology [COVID-19] Antigens Viral Coronavirus chemistry.chemical_classification Mutation Multidisciplinary Microbio genetics [SARS-CoV-2] spike protein SARS-CoV-2 Antigenic Variation Vaccination Spike Glycoprotein Coronavirus chemistry [Antigens Viral] ddc:500 Angiotensin-Converting Enzyme 2 Antibody chemistry [SARS-CoV-2] Protein Binding chemistry [Spike Glycoprotein Coronavirus] Coronavirus disease 2019 (COVID-19) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ACE2 protein human metabolism [Antibodies Neutralizing] Biology Receptor binding site Article Antigenic drift immunology [Antibodies Viral] Protein Domains Report medicine Humans metabolism [Receptors Coronavirus] Gene Immune Evasion Binding Sites metabolism [Antibodies Viral] immunology [Spike Glycoprotein Coronavirus] SARS-CoV-2 Biochem COVID-19 Virology immunology [Antigens Viral] Antibodies Neutralizing immunology [Antibodies Neutralizing] metabolism [Antigens Viral] Enzyme chemistry metabolism [Spike Glycoprotein Coronavirus] biology.protein Binding Sites Antibody Reports Receptors Coronavirus |
| Zdroj: | Science 373(6556), 818-823 (2021). doi:10.1126/science.abh1139 bioRxiv article-version (status) pre article-version (number) 1 Science, 373(6556), 818-823. American Association for the Advancement of Science Science (New York, N.y.) |
| ISSN: | 0036-8075 |
| DOI: | 10.1126/science.abh1139 |
| Popis: | The protective efficacy of neutralizing antibodies (nAbs) elicited during natural infection with SARS-CoV-2 and by vaccination based on its spike protein has been compromised with emergence of the recent SARS-CoV-2 variants. Residues E484 and K417 in the receptor-binding site (RBS) are both mutated in lineages first described in South Africa (B.1.351) and Brazil (B.1.1.28.1). The nAbs isolated from SARS-CoV-2 patients are preferentially encoded by certain heavy-chain germline genes and the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2) can each bind the RBS in two different binding modes. However, their binding and neutralization are abrogated by either the E484K or K417N mutation, whereas nAbs to the cross-reactive CR3022 and S309 sites are largely unaffected. This structural and functional analysis illustrates why mutations at E484 and K417 adversely affect major classes of nAbs to SARS-CoV-2 with consequences for next-generation COVID-19 vaccines. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |