| Autor: |
Leire de Campos-Mata, Benjamin Trinité, Andrea Modrego, Sonia Tejedor Vaquero, Edwards Pradenas, Anna Pons-Grífols, Natalia Rodrigo Melero, Diego Carlero, Silvia Marfil, César Santiago, Dàlia Raïch-Regué, María Teresa Bueno-Carrasco, Ferran Tarrés-Freixas, Ferran Abancó, Victor Urrea, Nuria Izquierdo-Useros, Eva Riveira-Muñoz, Ester Ballana, Mónica Pérez, Júlia Vergara-Alert, Joaquim Segalés, Carlo Carolis, Rocío Arranz, Julià Blanco, Giuliana Magri |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2041-1723 |
| DOI: |
10.1038/s41467-024-45171-9 |
| Popis: |
Abstract Here we report the characterization of 17T2, a SARS-CoV-2 pan-neutralizing human monoclonal antibody isolated from a COVID-19 convalescent individual infected during the first pandemic wave. 17T2 is a class 1 VH1-58/κ3-20 antibody, derived from a receptor binding domain (RBD)-specific IgA+ memory B cell, with a broad neutralizing activity against former and new SARS-CoV-2 variants, including XBB.1.16 and BA.2.86 Omicron subvariants. Consistently, 17T2 demonstrates in vivo prophylactic and therapeutic activity against Omicron BA.1.1 infection in K18-hACE2 mice. Cryo-electron microscopy reconstruction shows that 17T2 binds the BA.1 spike with the RBD in “up” position and blocks the receptor binding motif, as other structurally similar antibodies do, including S2E12. Yet, unlike S2E12, 17T2 retains its neutralizing activity against all variants tested, probably due to a larger RBD contact area. These results highlight the impact of small structural antibody changes on neutralizing performance and identify 17T2 as a potential candidate for future clinical interventions. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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