A monoclonal antibody targeting a large surface of the receptor binding motif shows pan-neutralizing SARS-CoV-2 activity

Leire 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 () and Giuliana Magri ()
Additional contact information
Leire Campos-Mata: Hospital del Mar Research Institute (IMIM)
Benjamin Trinité: Campus Can Ruti
Andrea Modrego: Centro Nacional de Biotecnología (CNB-CSIC)
Sonia Tejedor Vaquero: Hospital del Mar Research Institute (IMIM)
Edwards Pradenas: Campus Can Ruti
Anna Pons-Grífols: Campus Can Ruti
Natalia Rodrigo Melero: The Barcelona Institute of Science and Technology
Diego Carlero: Centro Nacional de Biotecnología (CNB-CSIC)
Silvia Marfil: Campus Can Ruti
César Santiago: Centro Nacional de Biotecnología (CNB-CSIC)
Dàlia Raïch-Regué: Campus Can Ruti
María Teresa Bueno-Carrasco: Centro Nacional de Biotecnología (CNB-CSIC)
Ferran Tarrés-Freixas: Campus Can Ruti
Ferran Abancó: Campus Can Ruti
Victor Urrea: Campus Can Ruti
Nuria Izquierdo-Useros: Campus Can Ruti
Eva Riveira-Muñoz: Campus Can Ruti
Ester Ballana: Campus Can Ruti
Mónica Pérez: Campus de la Universitat Autònoma de Barcelona (UAB)
Júlia Vergara-Alert: Campus de la Universitat Autònoma de Barcelona (UAB)
Joaquim Segalés: Campus de la Universitat Autònoma de Barcelona (UAB)
Carlo Carolis: The Barcelona Institute of Science and Technology
Rocío Arranz: Centro Nacional de Biotecnología (CNB-CSIC)
Julià Blanco: Campus Can Ruti
Giuliana Magri: Hospital del Mar Research Institute (IMIM)

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: 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.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-45171-9 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45171-9

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-45171-9

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().