دورية أكاديمية
Neutralization, effector function and immune imprinting of Omicron variants
| العنوان: | Neutralization, effector function and immune imprinting of Omicron variants |
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| المؤلفون: | Addetia, Amin, Piccoli, Luca, Case, James Brett, Park, Young-Jun, Beltramello, Martina, Guarino, Barbara, Dang, Ha, de Melo, Guilherme Dias, Pinto, Dora, Sprouse, Kaitlin, Scheaffer, Suzanne M, Bassi, Jessica, Silacci-Fregni, Chiara, Muoio, Francesco, Dini, Marco, Vincenzetti, Lucia, Acosta, Rima, Johnson, Daisy, Subramanian, Sambhavi, Saliba, Christian, Giurdanella, Martina, Lombardo, Gloria, Leoni, Giada, Culap, Katja, McAlister, Carley, Rajesh, Anushka, Dellota, Exequiel, Zhou, Jiayi, Farhat, Nisar, Bohan, Dana, Ceschi, Alessandro |
| المصدر: | Addetia, Amin; Piccoli, Luca; Case, James Brett; Park, Young-Jun; Beltramello, Martina; Guarino, Barbara; Dang, Ha; de Melo, Guilherme Dias; Pinto, Dora; Sprouse, Kaitlin; Scheaffer, Suzanne M; Bassi, Jessica; Silacci-Fregni, Chiara; Muoio, Francesco; Dini, Marco; Vincenzetti, Lucia; Acosta, Rima; Johnson, Daisy; Subramanian, Sambhavi; Saliba, Christian; Giurdanella, Martina; Lombardo, Gloria; Leoni, Giada; Culap, Katja; McAlister, Carley; Rajesh, Anushka; Dellota, Exequiel; Zhou, Jiayi; Farhat, Nisar; Bohan, Dana; Ceschi, Alessandro; et al (2023). Neutralization, effector function and immune imprinting of Omicron variants. Nature, 621(7979):592-601. |
| بيانات النشر: | Nature Publishing Group |
| سنة النشر: | 2023 |
| المجموعة: | University of Zurich (UZH): ZORA (Zurich Open Repository and Archive |
| مصطلحات موضوعية: | Clinic for Clinical Pharmacology and Toxicology, 610 Medicine & health, Multidisciplinary |
| الوصف: | Currently circulating SARS-CoV-2 variants have acquired convergent mutations at hot spots in the receptor-binding domain$^{1}$ (RBD) of the spike protein. The effects of these mutations on viral infection and transmission and the efficacy of vaccines and therapies remains poorly understood. Here we demonstrate that recently emerged BQ.1.1 and XBB.1.5 variants bind host ACE2 with high affinity and promote membrane fusion more efficiently than earlier Omicron variants. Structures of the BQ.1.1, XBB.1 and BN.1 RBDs bound to the fragment antigen-binding region of the S309 antibody (the parent antibody for sotrovimab) and human ACE2 explain the preservation of antibody binding through conformational selection, altered ACE2 recognition and immune evasion. We show that sotrovimab binds avidly to all Omicron variants, promotes Fc-dependent effector functions and protects mice challenged with BQ.1.1 and hamsters challenged with XBB.1.5. Vaccine-elicited human plasma antibodies cross-react with and trigger effector functions against current Omicron variants, despite a reduced neutralizing activity, suggesting a mechanism of protection against disease, exemplified by S309. Cross-reactive RBD-directed human memory B cells remained dominant even after two exposures to Omicron spikes, underscoring the role of persistent immune imprinting. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0028-0836 |
| العلاقة: | https://www.zora.uzh.ch/id/eprint/236265/1/ZORA_s41586_023_06487_6.pdfTest; info:pmid/37648855; urn:issn:0028-0836 |
| DOI: | 10.5167/uzh-236265 |
| DOI: | 10.1038/s41586-023-06487-6 |
| الإتاحة: | https://doi.org/10.5167/uzh-23626510.1038/s41586-023-06487-6Test https://www.zora.uzh.ch/id/eprint/236265Test/ https://www.zora.uzh.ch/id/eprint/236265/1/ZORA_s41586_023_06487_6.pdfTest |
| حقوق: | info:eu-repo/semantics/openAccess ; Creative Commons: Attribution 4.0 International (CC BY 4.0) ; http://creativecommons.org/licenses/by/4.0Test/ |
| رقم الانضمام: | edsbas.3B3264D1 |
| قاعدة البيانات: | BASE |
| تدمد: | 00280836 |
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| DOI: | 10.5167/uzh-236265 |