Show simple item record

dc.contributor.authorMonir, Ejemel
dc.contributor.authorLi, Qi
dc.contributor.authorHou, Shurong
dc.contributor.authorSchiller, Zachary
dc.contributor.authorWallace, Aaron
dc.contributor.authorAmcheslavsky, Alla
dc.contributor.authorYilmaz, Nese Kurt
dc.contributor.authorToomey, Jacqueline R.
dc.contributor.authorSchneider, Ryan
dc.contributor.authorRamchetty, Anudeep S.
dc.contributor.authorGanesa, Chandrashekar
dc.contributor.authorCavacini, Lisa
dc.contributor.authorKlempner, Mark S.
dc.contributor.authorSchiffer, Celia A.
dc.contributor.authorWang, Yan
dc.date2022-08-11T08:08:09.000
dc.date.accessioned2022-08-23T15:44:27Z
dc.date.available2022-08-23T15:44:27Z
dc.date.issued2020-08-21
dc.date.submitted2020-08-27
dc.identifier.citation<p>Ejemel M, Li Q, Hou S, Schiller ZA, Tree JA, Wallace A, Amcheslavsky A, Kurt Yilmaz N, Buttigieg KR, Elmore MJ, Godwin K, Coombes N, Toomey JR, Schneider R, Ramchetty AS, Close BJ, Chen DY, Conway HL, Saeed M, Ganesa C, Carroll MW, Cavacini LA, Klempner MS, Schiffer CA, Wang Y. A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction. Nat Commun. 2020 Aug 21;11(1):4198. doi: 10.1038/s41467-020-18058-8. PMID: 32826914. <a href="https://doi.org/10.1038/s41467-020-18058-8">Link to article on publisher's site</a></p>
dc.identifier.issn2041-1723 (Linking)
dc.identifier.doi10.1038/s41467-020-18058-8
dc.identifier.pmid32826914
dc.identifier.urihttp://hdl.handle.net/20.500.14038/27317
dc.description<p>Full author list omitted for brevity. For the full list of authors, see article.</p>
dc.description.abstractCOVID-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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=32826914&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights© The Author(s) 2020. Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectCOVID-19
dc.subjectSARS-CoV-2
dc.subjectAntibody therapy
dc.subjectMolecular modelling
dc.subjectMucosal immunology
dc.subjectViral infection
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry
dc.subjectImmunity
dc.subjectImmunology of Infectious Disease
dc.subjectImmunopathology
dc.subjectImmunoprophylaxis and Therapy
dc.subjectImmunotherapy
dc.subjectInfectious Disease
dc.subjectMicrobiology
dc.subjectVirus Diseases
dc.titleA cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction
dc.typeJournal Article
dc.source.journaltitleNature communications
dc.source.volume11
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1104&amp;context=covid19&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/covid19/102
dc.identifier.contextkey19160743
refterms.dateFOA2022-08-23T15:44:27Z
html.description.abstract<p>COVID-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.</p>
dc.identifier.submissionpathcovid19/102
dc.contributor.departmentSchiffer Lab
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentMassBiologics
dc.source.pages4198


Files in this item

Thumbnail
Name:
s41467_020_18058_8.pdf
Size:
1.460Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record

© The Author(s) 2020. Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
Except where otherwise noted, this item's license is described as © The Author(s) 2020. Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.