Potent neutralization by a receptor binding domain monoclonal antibody with broad specificity for SARS-CoV-2 JN.1 and other variants
Rattachement africain : us, Égypte. Niveau de preuve : code pays fourni par la source.
Le résumé fourni par la source
SARS-CoV-2 continues to be a public health burden, driven in-part by its continued antigenic diversification and resulting emergence of new variants. While increasing herd immunity, current vaccines, and therapeutics have improved outcomes for some; prophylactic and treatment interventions that are not compromised by viral evolution of the Spike protein are still needed. Using a rationally designed SARS-CoV-2 Receptor Binding Domain (RBD) - ACE2 fusion protein and differential selection process with native Omicron RBD protein, we developed a recombinant human monoclonal antibody (hmAb) from a convalescent individual following SARS-CoV-2 Omicron infection. The resulting hmAb, 1301B7 potently neutralized a wide range of SARS-CoV-2 variants including the original Wuhan and more recent Omicron JN.1 strain, as well as SARS-CoV. Structure determination of the SARS-CoV-2 EG5.1 Spike/1301B7 Fab complex by cryo-electron microscopy at 3.1Å resolution demonstrates 1301B7 contacts the ACE2 binding site of RBD exclusively through its VH1-69 heavy chain, making contacts using CDRs1-3, as well as framework region 3 (FR3). Broad specificity is achieved through 1301B7 binding to many conserved residues of Omicron variants including Y501 and H505. Consistent with its extensive binding epitope, 1301B7 is able to potently diminish viral burden in the upper and lower respiratory tract and protect mice from challenge with Omicron XBB1.5 and Omicron JN.1 viruses. These results suggest 1301B7 has broad potential to prevent or treat clinical SARS-CoV-2 infections and to guide development of RBD-based universal SARS-CoV-2 prophylactic vaccines and therapeutic approaches.
Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.
Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Potent neutralization by a receptor binding domain monoclonal antibody with broad specificity for SARS-CoV-2 JN.1 and other variants
- Date Crossref
- 29/04/2024
- Éditeur
- openRxiv
- Type
- posted-content
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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University of Alabama at Birmingham Department of Medicine pays non établi dans la noticeUniversité ou école supérieure
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Texas Biomedical Research Institute Department of Disease Intervention and Prevention pays non établi dans la noticeStructure de recherche
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Zagazig University Zagazig University, Égypte (code pays fourni par la source)Université ou école supérieure
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Pacific Northwest University of Health Sciences pays non établi dans la noticeUniversité ou école supérieure
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National Research Centre Center of Scientific Excellence for Influenza Viruses Giza, Égypte (code pays fourni par la source)Structure de recherche
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Aaron Diamond AIDS Research Center pays non établi dans la noticeStructure de recherche
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Columbia University Aaron Diamond AIDS Research Center pays non établi dans la noticeUniversité ou école supérieure
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Faculty of Veterinary Medicine Department of Zoonotic Diseases Zagazig University, Égypte (pays nommé en fin d’affiliation)Université ou école supérieure
Department of Medicine — University of Alabama at Birmingham, Department of Disease Intervention and Prevention — Texas Biomedical Research Institute et Zagazig University (Zagazig University, Égypte), avec 5 autres affiliations. Pays d’affiliation : Égypte.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.