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An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models
Broadly neutralizing antibodies are an important treatment for individuals with coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Antibody-based therapeutics are also essential for pandemic preparedness against future Sarbecovirus outbreaks....
| Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American Association for the Advancement of Science
2021
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9924070/ https://www.ncbi.nlm.nih.gov/pubmed/34609205 http://dx.doi.org/10.1126/scitranslmed.abi7826 |
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| author | Schepens, Bert van Schie, Loes Nerinckx, Wim Roose, Kenny Van Breedam, Wander Fijalkowska, Daria Devos, Simon Weyts, Wannes De Cae, Sieglinde Vanmarcke, Sandrine Lonigro, Chiara Eeckhaut, Hannah Van Herpe, Dries Borloo, Jimmy Oliveira, Ana Filipa Catani, João Paulo Portela Creytens, Sarah De Vlieger, Dorien Michielsen, Gitte Marchan, Jackeline Cecilia Zavala Moschonas, George D. Rossey, Iebe Sedeyn, Koen Van Hecke, Annelies Zhang, Xin Langendries, Lana Jacobs, Sofie ter Horst, Sebastiaan Seldeslachts, Laura Liesenborghs, Laurens Boudewijns, Robbert Thibaut, Hendrik Jan Dallmeier, Kai Velde, Greetje Vande Weynand, Birgit Beer, Julius Schnepf, Daniel Ohnemus, Annette Remory, Isabel Foo, Caroline S. Abdelnabi, Rana Maes, Piet Kaptein, Suzanne J. F. Rocha-Pereira, Joana Jochmans, Dirk Delang, Leen Peelman, Frank Staeheli, Peter Schwemmle, Martin Devoogdt, Nick Tersago, Dominique Germani, Massimiliano Heads, James Henry, Alistair Popplewell, Andrew Ellis, Mark Brady, Kevin Turner, Alison Dombrecht, Bruno Stortelers, Catelijne Neyts, Johan Callewaert, Nico Saelens, Xavier |
| author_facet | Schepens, Bert van Schie, Loes Nerinckx, Wim Roose, Kenny Van Breedam, Wander Fijalkowska, Daria Devos, Simon Weyts, Wannes De Cae, Sieglinde Vanmarcke, Sandrine Lonigro, Chiara Eeckhaut, Hannah Van Herpe, Dries Borloo, Jimmy Oliveira, Ana Filipa Catani, João Paulo Portela Creytens, Sarah De Vlieger, Dorien Michielsen, Gitte Marchan, Jackeline Cecilia Zavala Moschonas, George D. Rossey, Iebe Sedeyn, Koen Van Hecke, Annelies Zhang, Xin Langendries, Lana Jacobs, Sofie ter Horst, Sebastiaan Seldeslachts, Laura Liesenborghs, Laurens Boudewijns, Robbert Thibaut, Hendrik Jan Dallmeier, Kai Velde, Greetje Vande Weynand, Birgit Beer, Julius Schnepf, Daniel Ohnemus, Annette Remory, Isabel Foo, Caroline S. Abdelnabi, Rana Maes, Piet Kaptein, Suzanne J. F. Rocha-Pereira, Joana Jochmans, Dirk Delang, Leen Peelman, Frank Staeheli, Peter Schwemmle, Martin Devoogdt, Nick Tersago, Dominique Germani, Massimiliano Heads, James Henry, Alistair Popplewell, Andrew Ellis, Mark Brady, Kevin Turner, Alison Dombrecht, Bruno Stortelers, Catelijne Neyts, Johan Callewaert, Nico Saelens, Xavier |
| author_sort | Schepens, Bert |
| collection | PubMed |
| description | Broadly neutralizing antibodies are an important treatment for individuals with coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Antibody-based therapeutics are also essential for pandemic preparedness against future Sarbecovirus outbreaks. Camelid-derived single domain antibodies (VHHs) exhibit potent antimicrobial activity and are being developed as SARS-CoV-2–neutralizing antibody-like therapeutics. Here, we identified VHHs that neutralize both SARS-CoV-1 and SARS-CoV-2, including now circulating variants. We observed that the VHHs bound to a highly conserved epitope in the receptor binding domain of the viral spike protein that is difficult to access for human antibodies. Structure-guided molecular modeling, combined with rapid yeast-based prototyping, resulted in an affinity enhanced VHH-human immunoglobulin G1 Fc fusion molecule with subnanomolar neutralizing activity. This VHH-Fc fusion protein, produced in and purified from cultured Chinese hamster ovary cells, controlled SARS-CoV-2 replication in prophylactic and therapeutic settings in mice expressing human angiotensin converting enzyme 2 and in hamsters infected with SARS-CoV-2. These data led to affinity-enhanced selection of the VHH, XVR011, a stable anti–COVID-19 biologic that is now being evaluated in the clinic. |
| format | Online Article Text |
| id | pubmed-9924070 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2021 |
| publisher | American Association for the Advancement of Science |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-99240702023-02-17 An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models Schepens, Bert van Schie, Loes Nerinckx, Wim Roose, Kenny Van Breedam, Wander Fijalkowska, Daria Devos, Simon Weyts, Wannes De Cae, Sieglinde Vanmarcke, Sandrine Lonigro, Chiara Eeckhaut, Hannah Van Herpe, Dries Borloo, Jimmy Oliveira, Ana Filipa Catani, João Paulo Portela Creytens, Sarah De Vlieger, Dorien Michielsen, Gitte Marchan, Jackeline Cecilia Zavala Moschonas, George D. Rossey, Iebe Sedeyn, Koen Van Hecke, Annelies Zhang, Xin Langendries, Lana Jacobs, Sofie ter Horst, Sebastiaan Seldeslachts, Laura Liesenborghs, Laurens Boudewijns, Robbert Thibaut, Hendrik Jan Dallmeier, Kai Velde, Greetje Vande Weynand, Birgit Beer, Julius Schnepf, Daniel Ohnemus, Annette Remory, Isabel Foo, Caroline S. Abdelnabi, Rana Maes, Piet Kaptein, Suzanne J. F. Rocha-Pereira, Joana Jochmans, Dirk Delang, Leen Peelman, Frank Staeheli, Peter Schwemmle, Martin Devoogdt, Nick Tersago, Dominique Germani, Massimiliano Heads, James Henry, Alistair Popplewell, Andrew Ellis, Mark Brady, Kevin Turner, Alison Dombrecht, Bruno Stortelers, Catelijne Neyts, Johan Callewaert, Nico Saelens, Xavier Sci Transl Med Research Articles Broadly neutralizing antibodies are an important treatment for individuals with coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Antibody-based therapeutics are also essential for pandemic preparedness against future Sarbecovirus outbreaks. Camelid-derived single domain antibodies (VHHs) exhibit potent antimicrobial activity and are being developed as SARS-CoV-2–neutralizing antibody-like therapeutics. Here, we identified VHHs that neutralize both SARS-CoV-1 and SARS-CoV-2, including now circulating variants. We observed that the VHHs bound to a highly conserved epitope in the receptor binding domain of the viral spike protein that is difficult to access for human antibodies. Structure-guided molecular modeling, combined with rapid yeast-based prototyping, resulted in an affinity enhanced VHH-human immunoglobulin G1 Fc fusion molecule with subnanomolar neutralizing activity. This VHH-Fc fusion protein, produced in and purified from cultured Chinese hamster ovary cells, controlled SARS-CoV-2 replication in prophylactic and therapeutic settings in mice expressing human angiotensin converting enzyme 2 and in hamsters infected with SARS-CoV-2. These data led to affinity-enhanced selection of the VHH, XVR011, a stable anti–COVID-19 biologic that is now being evaluated in the clinic. American Association for the Advancement of Science 2021-11-24 /pmc/articles/PMC9924070/ /pubmed/34609205 http://dx.doi.org/10.1126/scitranslmed.abi7826 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| spellingShingle | Research Articles Schepens, Bert van Schie, Loes Nerinckx, Wim Roose, Kenny Van Breedam, Wander Fijalkowska, Daria Devos, Simon Weyts, Wannes De Cae, Sieglinde Vanmarcke, Sandrine Lonigro, Chiara Eeckhaut, Hannah Van Herpe, Dries Borloo, Jimmy Oliveira, Ana Filipa Catani, João Paulo Portela Creytens, Sarah De Vlieger, Dorien Michielsen, Gitte Marchan, Jackeline Cecilia Zavala Moschonas, George D. Rossey, Iebe Sedeyn, Koen Van Hecke, Annelies Zhang, Xin Langendries, Lana Jacobs, Sofie ter Horst, Sebastiaan Seldeslachts, Laura Liesenborghs, Laurens Boudewijns, Robbert Thibaut, Hendrik Jan Dallmeier, Kai Velde, Greetje Vande Weynand, Birgit Beer, Julius Schnepf, Daniel Ohnemus, Annette Remory, Isabel Foo, Caroline S. Abdelnabi, Rana Maes, Piet Kaptein, Suzanne J. F. Rocha-Pereira, Joana Jochmans, Dirk Delang, Leen Peelman, Frank Staeheli, Peter Schwemmle, Martin Devoogdt, Nick Tersago, Dominique Germani, Massimiliano Heads, James Henry, Alistair Popplewell, Andrew Ellis, Mark Brady, Kevin Turner, Alison Dombrecht, Bruno Stortelers, Catelijne Neyts, Johan Callewaert, Nico Saelens, Xavier An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title | An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title_full | An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title_fullStr | An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title_full_unstemmed | An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title_short | An affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against SARS-CoV-2 infection in animal models |
| title_sort | affinity-enhanced, broadly neutralizing heavy chain–only antibody protects against sars-cov-2 infection in animal models |
| topic | Research Articles |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9924070/ https://www.ncbi.nlm.nih.gov/pubmed/34609205 http://dx.doi.org/10.1126/scitranslmed.abi7826 |
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