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Fc-Independent Protection from SARS-CoV-2 Infection by Recombinant Human Monoclonal Antibodies
The use of passively-administered neutralizing antibodies is a promising approach for the prevention and treatment of SARS-CoV-2 infection. Antibody-mediated protection may involve immune system recruitment through Fc-dependent activation of effector cells and the complement system. However, the rol...
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Published in: | Antibodies (Basel) 2021-11, Vol.10 (4), p.45 |
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creator | Noy-Porat, Tal Edri, Avishay Alcalay, Ron Makdasi, Efi Gur, David Aftalion, Moshe Evgy, Yentl Beth-Din, Adi Levy, Yinon Epstein, Eyal Radinsky, Olga Zauberman, Ayelet Lazar, Shirley Yitzhaki, Shmuel Marcus, Hadar Porgador, Angel Rosenfeld, Ronit Mazor, Ohad |
description | The use of passively-administered neutralizing antibodies is a promising approach for the prevention and treatment of SARS-CoV-2 infection. Antibody-mediated protection may involve immune system recruitment through Fc-dependent activation of effector cells and the complement system. However, the role of Fc-mediated functions in the efficacious in-vivo neutralization of SARS-CoV-2 is not yet clear, and it is of high importance to delineate the role this process plays in antibody-mediated protection. Toward this aim, we have chosen two highly potent SARS-CoV-2 neutralizing human monoclonal antibodies, MD65 and BLN1 that target distinct domains of the spike (RBD and NTD, respectively). The Fc of these antibodies was engineered to include the triple mutation N297G/S298G/T299A that eliminates glycosylation and the binding to FcγR and to the complement system activator C1q. As expected, the virus neutralization activity (in-vitro) of the engineered antibodies was retained. To study the role of Fc-mediated functions, the protective activity of these antibodies was tested against lethal SARS-CoV-2 infection of K18-hACE2 transgenic mice, when treatment was initiated either before or two days post-exposure. Antibody treatment with both Fc-variants similarly rescued the mice from death reduced viral load and prevented signs of morbidity. Taken together, this work provides important insight regarding the contribution of Fc-effector functions in MD65 and BLN1 antibody-mediated protection, which should aid in the future design of effective antibody-based therapies. |
doi_str_mv | 10.3390/antib10040045 |
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Antibody-mediated protection may involve immune system recruitment through Fc-dependent activation of effector cells and the complement system. However, the role of Fc-mediated functions in the efficacious in-vivo neutralization of SARS-CoV-2 is not yet clear, and it is of high importance to delineate the role this process plays in antibody-mediated protection. Toward this aim, we have chosen two highly potent SARS-CoV-2 neutralizing human monoclonal antibodies, MD65 and BLN1 that target distinct domains of the spike (RBD and NTD, respectively). The Fc of these antibodies was engineered to include the triple mutation N297G/S298G/T299A that eliminates glycosylation and the binding to FcγR and to the complement system activator C1q. As expected, the virus neutralization activity (in-vitro) of the engineered antibodies was retained. To study the role of Fc-mediated functions, the protective activity of these antibodies was tested against lethal SARS-CoV-2 infection of K18-hACE2 transgenic mice, when treatment was initiated either before or two days post-exposure. Antibody treatment with both Fc-variants similarly rescued the mice from death reduced viral load and prevented signs of morbidity. Taken together, this work provides important insight regarding the contribution of Fc-effector functions in MD65 and BLN1 antibody-mediated protection, which should aid in the future design of effective antibody-based therapies.</description><identifier>ISSN: 2073-4468</identifier><identifier>EISSN: 2073-4468</identifier><identifier>DOI: 10.3390/antib10040045</identifier><identifier>PMID: 34842604</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>a-glycosylated ; Antigens ; Cell activation ; Cell culture ; Complement activation ; Complement component C1q ; Coronaviruses ; COVID-19 ; Ebola virus ; Effector cells ; fragment crystallizable (Fc) ; Glycosylation ; Immune system ; Infections ; Interferometry ; K18-hACE2 ; Monoclonal antibodies ; monoclonal antibodies (mAbs) ; Morbidity ; Mutation ; Neutralization ; Neutralizing ; Pandemics ; Proteins ; SARS-CoV-2 ; Sensors ; Severe acute respiratory syndrome coronavirus 2 ; Transgenic mice ; Viral diseases</subject><ispartof>Antibodies (Basel), 2021-11, Vol.10 (4), p.45</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-eb883a6cc7e9575edadf98c48a0bcff76f5e235c380fc6abea787db895c4a1673</citedby><cites>FETCH-LOGICAL-c524t-eb883a6cc7e9575edadf98c48a0bcff76f5e235c380fc6abea787db895c4a1673</cites><orcidid>0000-0003-1276-0464 ; 0000-0001-5956-9865 ; 0000-0002-9602-2532 ; 0000-0003-2750-5394</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2612725057/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2612725057?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids></links><search><creatorcontrib>Noy-Porat, Tal</creatorcontrib><creatorcontrib>Edri, Avishay</creatorcontrib><creatorcontrib>Alcalay, Ron</creatorcontrib><creatorcontrib>Makdasi, Efi</creatorcontrib><creatorcontrib>Gur, David</creatorcontrib><creatorcontrib>Aftalion, Moshe</creatorcontrib><creatorcontrib>Evgy, Yentl</creatorcontrib><creatorcontrib>Beth-Din, Adi</creatorcontrib><creatorcontrib>Levy, Yinon</creatorcontrib><creatorcontrib>Epstein, Eyal</creatorcontrib><creatorcontrib>Radinsky, Olga</creatorcontrib><creatorcontrib>Zauberman, Ayelet</creatorcontrib><creatorcontrib>Lazar, Shirley</creatorcontrib><creatorcontrib>Yitzhaki, Shmuel</creatorcontrib><creatorcontrib>Marcus, Hadar</creatorcontrib><creatorcontrib>Porgador, Angel</creatorcontrib><creatorcontrib>Rosenfeld, Ronit</creatorcontrib><creatorcontrib>Mazor, Ohad</creatorcontrib><title>Fc-Independent Protection from SARS-CoV-2 Infection by Recombinant Human Monoclonal Antibodies</title><title>Antibodies (Basel)</title><description>The use of passively-administered neutralizing antibodies is a promising approach for the prevention and treatment of SARS-CoV-2 infection. Antibody-mediated protection may involve immune system recruitment through Fc-dependent activation of effector cells and the complement system. However, the role of Fc-mediated functions in the efficacious in-vivo neutralization of SARS-CoV-2 is not yet clear, and it is of high importance to delineate the role this process plays in antibody-mediated protection. Toward this aim, we have chosen two highly potent SARS-CoV-2 neutralizing human monoclonal antibodies, MD65 and BLN1 that target distinct domains of the spike (RBD and NTD, respectively). The Fc of these antibodies was engineered to include the triple mutation N297G/S298G/T299A that eliminates glycosylation and the binding to FcγR and to the complement system activator C1q. As expected, the virus neutralization activity (in-vitro) of the engineered antibodies was retained. To study the role of Fc-mediated functions, the protective activity of these antibodies was tested against lethal SARS-CoV-2 infection of K18-hACE2 transgenic mice, when treatment was initiated either before or two days post-exposure. Antibody treatment with both Fc-variants similarly rescued the mice from death reduced viral load and prevented signs of morbidity. 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Antibody-mediated protection may involve immune system recruitment through Fc-dependent activation of effector cells and the complement system. However, the role of Fc-mediated functions in the efficacious in-vivo neutralization of SARS-CoV-2 is not yet clear, and it is of high importance to delineate the role this process plays in antibody-mediated protection. Toward this aim, we have chosen two highly potent SARS-CoV-2 neutralizing human monoclonal antibodies, MD65 and BLN1 that target distinct domains of the spike (RBD and NTD, respectively). The Fc of these antibodies was engineered to include the triple mutation N297G/S298G/T299A that eliminates glycosylation and the binding to FcγR and to the complement system activator C1q. As expected, the virus neutralization activity (in-vitro) of the engineered antibodies was retained. To study the role of Fc-mediated functions, the protective activity of these antibodies was tested against lethal SARS-CoV-2 infection of K18-hACE2 transgenic mice, when treatment was initiated either before or two days post-exposure. Antibody treatment with both Fc-variants similarly rescued the mice from death reduced viral load and prevented signs of morbidity. Taken together, this work provides important insight regarding the contribution of Fc-effector functions in MD65 and BLN1 antibody-mediated protection, which should aid in the future design of effective antibody-based therapies.</abstract><cop>Basel</cop><pub>MDPI AG</pub><pmid>34842604</pmid><doi>10.3390/antib10040045</doi><orcidid>https://orcid.org/0000-0003-1276-0464</orcidid><orcidid>https://orcid.org/0000-0001-5956-9865</orcidid><orcidid>https://orcid.org/0000-0002-9602-2532</orcidid><orcidid>https://orcid.org/0000-0003-2750-5394</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | a-glycosylated Antigens Cell activation Cell culture Complement activation Complement component C1q Coronaviruses COVID-19 Ebola virus Effector cells fragment crystallizable (Fc) Glycosylation Immune system Infections Interferometry K18-hACE2 Monoclonal antibodies monoclonal antibodies (mAbs) Morbidity Mutation Neutralization Neutralizing Pandemics Proteins SARS-CoV-2 Sensors Severe acute respiratory syndrome coronavirus 2 Transgenic mice Viral diseases |
title | Fc-Independent Protection from SARS-CoV-2 Infection by Recombinant Human Monoclonal Antibodies |
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