DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jeong, Bo-Seong | ko |
dc.contributor.author | Jeon, Joon Young | ko |
dc.contributor.author | Lai, Chih-Jen | ko |
dc.contributor.author | Yun, Hye-Yeoung | ko |
dc.contributor.author | Jung, Jae U | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2022-12-22T02:01:29Z | - |
dc.date.available | 2022-12-22T02:01:29Z | - |
dc.date.created | 2022-12-21 | - |
dc.date.created | 2022-12-21 | - |
dc.date.created | 2022-12-21 | - |
dc.date.created | 2022-12-21 | - |
dc.date.created | 2022-12-21 | - |
dc.date.issued | 2022-11 | - |
dc.identifier.citation | FRONTIERS IN IMMUNOLOGY, v.13 | - |
dc.identifier.issn | 1664-3224 | - |
dc.identifier.uri | http://hdl.handle.net/10203/303471 | - |
dc.description.abstract | More than 80% of SARS-CoV-2 variants, including Alpha and Omicron, contain an N501Y mutation in the receptor-binding domain (RBD) of the spike protein. The N501Y change is an adaptive mutation enabling tighter interaction with the human ACE2 receptor. We have developed a broadly neutralizing antibody (nAb), D27LEY, whose binding affinity was intentionally optimized for Y501. This N501Y-centric antibody not only interacts with the Y501-containing RBDs of SARS-CoV-2 variants, including Omicron, with pico- or subnanomolar binding affinity, but also binds tightly to the RBDs with a different amino acid at residue 501. The crystal structure of the Fab fragment of D27LEY bound to the RBD of the Alpha variant reveals that the Y501-containing loop adopts a ribbon-like topology and serves as a small but major epitope in which Y501 is a part of extensive intermolecular interactions. A hydrophobic cleft on the most conserved surface of the RBD core serves as another major binding epitope. These data explain the broad and potent cross-reactivity of this N501Y-centric antibody, and suggest that a vaccine antigenic component composed of the RBD core and a part of receptor-binding motif (RBM) containing tyrosine at residue 501 might elicit broad and potent humoral responses across sarbecoviruses. Copyright © 2022 Jeong, Jeon, Lai, Yun, Jung and Oh. | - |
dc.language | English | - |
dc.publisher | FRONTIERS MEDIA SA | - |
dc.title | Structural basis for the broad and potent cross-reactivity of an N501Y-centric antibody against sarbecoviruses | - |
dc.type | Article | - |
dc.identifier.wosid | 000900812500001 | - |
dc.identifier.scopusid | 2-s2.0-85143353705 | - |
dc.type.rims | ART | - |
dc.citation.volume | 13 | - |
dc.citation.publicationname | FRONTIERS IN IMMUNOLOGY | - |
dc.identifier.doi | 10.3389/fimmu.2022.1049867 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Jeon, Joon Young | - |
dc.contributor.nonIdAuthor | Lai, Chih-Jen | - |
dc.contributor.nonIdAuthor | Yun, Hye-Yeoung | - |
dc.contributor.nonIdAuthor | Jung, Jae U | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | broad-spectrum vaccine | - |
dc.subject.keywordAuthor | broadly neutralizing antibody | - |
dc.subject.keywordAuthor | computational affinity maturation | - |
dc.subject.keywordAuthor | key epitope | - |
dc.subject.keywordAuthor | SARS-CoV-2 | - |
dc.subject.keywordAuthor | viral evolution | - |
dc.subject.keywordPlus | RECEPTOR-BINDING DOMAIN | - |
dc.subject.keywordPlus | X-RAY | - |
dc.subject.keywordPlus | SARS-COV-2 | - |
dc.subject.keywordPlus | B.1.1.7 | - |
dc.subject.keywordPlus | LINEAGE | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.