Antibody evasion by the P.1 strain of SARS-CoV-2
| Autor: | Beibei Wang, D. Zhou, Elizabeth E. Fry, Julian C. Knight, Amy Flaxman, Valdinete Alves do Nascimento, Alexander J. Mentzer, E Barnes, Alex Pauvolid-Corrêa, Sarah C. Gilbert, M Bittaye, Mark A. Williams, Hulswit Rjg., Gavin R. Screaton, Sandra Belij-Rammerstorfer, Chang Liu, Andrew J. Pollard, David R. Hall, Tao Dong, David I. Stuart, Christina Dold, Felipe Gomes Naveca, Wanwisa Dejnirattisai, Elizabeth A. Clutterbuck, Paul Klenerman, Neil G. Paterson, Helen M. Ginn, C Fernandes da Costa, R Levin, Jingshan Ren, Duyvesteyn Hme., Thomas S. Walter, Aekkachai Tuekprakhon, Miles W. Carroll, Donal T. Skelly, R Nutalai, Yuguang Zhao, Thomas A. Bowden, D W Crook, S A Costa Clemens, Marilda M. Siqueira, P Supasa, Susanna Dunachie, S Bibi, Teresa Lambe, Paola Cristina Resende, Cesar Lopez-Camacho, J Slon-Campos, Juthathip Mongkolsapaya, Fabrícia F. Nascimento |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
medicine.drug_class
medicine.disease_cause Monoclonal antibody Immunoglobulin light chain Antibodies Viral General Biochemistry Genetics and Molecular Biology Virus Neutralization Article Cell Line 03 medical and health sciences 0302 clinical medicine Protein Domains medicine Humans Binding site Neutralizing antibody COVID-19 Serotherapy 030304 developmental biology Immune Evasion Sequence Deletion 0303 health sciences Mutation Vaccines Binding Sites biology SARS-CoV-2 Vaccination Immunization Passive Antibodies Monoclonal COVID-19 Virology Antibodies Neutralizing Spike Glycoprotein Coronavirus biology.protein Antibody 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Cell |
| Popis: | Terminating the SARS-CoV-2 pandemic relies upon pan-global vaccination. Current vaccines elicit neutralizing antibody responses to the virus spike derived from early isolates. However, new strains have emerged with multiple mutations: P.1 from Brazil, B.1.351 from South Africa and B.1.1.7 from the UK (12, 10 and 9 changes in the spike respectively). All have mutations in the ACE2 binding site with P.1 and B.1.351 having a virtually identical triplet: E484K, K417N/T and N501Y, which we show confer similar increased affinity for ACE2. We show that, surprisingly, P.1 is significantly less resistant to naturally acquired or vaccine induced antibody responses than B.1.351 suggesting that changes outside the RBD impact neutralisation. Monoclonal antibody 222 neutralises all three variants despite interacting with two of the ACE2 binding site mutations, we explain this through structural analysis and use the 222 light chain to largely restore neutralization potency to a major class of public antibodies. Structural and functional analysis of the P.1 variant of SARS-CoV-2 from Brazil reveals less resistance to antibodies generated from natural infection or vaccination compared to another similar variant, B.1.351. A monoclonal antibody mAb 222 is able to neutralize all three variants (P.1, B.1.351 and B.1.1.7), with its light chain able to restore neutralization potency to broad group of antibodies. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|