A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction

Vista sencilla de ítem
dc.creatorEjemel, Monir
dc.creatorLi, Qi
dc.creatorHou, Shurong
dc.creatorSchiller, Zachary A.
dc.creatorTree, Julia A.
dc.creatorWallace, Aaron
dc.creatorAmcheslavsky, Alla
dc.creatorKurt Yilmaz, Nese
dc.creatorButtigieg, Karen R.
dc.creatorElmore, Michael J.
dc.creatorGodwin, Kerry
dc.creatorCoombes, Naomi
dc.creatorToomey, Jacqueline R.
dc.creatorSchneider, Ryan
dc.creatorRamchetty, Anudeep S.
dc.creatorClose, Brianna J.
dc.creatorChen, Da Yuan
dc.creatorConway, Hasahn L.
dc.creatorSaeed, Mohsan
dc.creatorGanesa, Chandrashekar
dc.creatorCarroll, Miles W.
dc.creatorCavacini, Lisa A.
dc.creatorKlempner, Mark S.
dc.creatorSchiffer, Celia A.
dc.creatorWang, Yang
dc.date.accessioned2020-09-18T02:41:18Z
dc.date.available2020-09-18T02:41:18Z
dc.date.created2020-08-21
dc.description.abstractenglishCOVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity, or as a therapeutic, has yet been developed to SARS-CoV-2. In this study, we discover and characterize a cross-reactive human IgA monoclonal antibody, MAb362. MAb362 binds to both SARS-CoV and SARS-CoV-2 spike proteins and competitively blocks ACE2 receptor binding, by overlapping the ACE2 structural binding epitope. Furthermore, MAb362 IgA neutralizes both pseudotyped SARS-CoV and SARS-CoV-2 in 293 cells expressing ACE2. When converted to secretory IgA, MAb326 also neutralizes authentic SARS-CoV-2 virus while the IgG isotype shows no neutralization. Our results suggest that SARS-CoV-2 specific IgA antibodies, such as MAb362, may provide effective immunity against SARS-CoV-2 by inducing mucosal immunity within the respiratory system, a potentially critical feature of an effective vaccine.spa
dc.format.extent9 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.identifier.doihttps://doi.org/10.1038/s41467-020-18058-8spa
dc.identifier.issn2041-1723spa
dc.identifier.otherhttps://www.nature.com/articles/s41467-020-18058-8spa
dc.identifier.urihttps://hdl.handle.net/20.500.12010/13430
dc.language.isoengspa
dc.publisherNature Communicationsspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.localAbierto (Texto Completo)spa
dc.sourcereponame:Expeditio Repositorio Institucional UJTLspa
dc.sourceinstname:Universidad de Bogotá Jorge Tadeo Lozanospa
dc.subjectSARS-CoV-2spa
dc.subject.lembSíndrome respiratorio agudo gravespa
dc.subject.lembCOVID-19spa
dc.subject.lembSARS-CoV-2spa
dc.subject.lembCoronavirusspa
dc.titleA cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interactionspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersionspa
dc.type.localArtículospa

Archivos

Bloque original

Mostrando 1 - 1 de 1
Miniatura
Nombre:
s41467-020-18058-8.pdf
Tamaño:
1.46 MB
Formato:
Adobe Portable Document Format
Descripción:
Ver documento
Descargar

Bloque de licencias

Mostrando 1 - 1 de 1
Miniatura
Nombre:
license.txt
Tamaño:
2.87 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar

Colecciones

Documentos científicos relacionados a la COVID-19

Carrera 4 # 22-61 Teléfono: (+57) 601 242 7030 - 018000111022 Fax: (+57) 601 561 2107 Bogotá D.C., Colombia

Fundación Universitaria de Bogotá Jorge Tadeo Lozano | Vigilada Mineducación

Institución de educación superior privada, de utilidad común, sin ánimo de lucro y su carácter académico es el de Universidad

Reconocimiento personería jurídica: Resolución 2613 del 14 de agosto de 1959 Minjusticia.

Institución de Educación Superior sujeta a inspección y vigilancia por el Ministerio de Educación Nacional.

Software DSpace copyright © 2002-2026 LYRASIS