De novo protein design enables the precise induction of RSV-neutralizing antibodies
De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines...
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| Published in: | IDEAS Working Paper Series from RePEc Vol. 368; no. 6492 |
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| Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format: | Journal Article Paper |
| Language: | English |
| Published: |
United States
Federal Reserve Bank of St. Louis
15.05.2020
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| ISSN: | 1095-9203, 1095-9203 |
| Online Access: | Get full text |
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| Abstract | De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs. |
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| AbstractList | De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs.De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs. De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs. Copyright De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a major methodological challenge. In vaccinology, the induction of precise antibody responses remains a cornerstone for next-generation vaccines. Here, we present a protein design algorithm called TopoBuilder, with which we engineered epitope-focused immunogens displaying complex structural motifs. In both mice and nonhuman primates, cocktails of three de novo-designed immunogens induced robust neutralizing responses against the respiratory syncytial virus. Furthermore, the immunogens refocused preexisting antibody responses toward defined neutralization epitopes. Overall, our design approach opens the possibility of targeting specific epitopes for the development of vaccines and therapeutic antibodies and, more generally, will be applicable to the design of de novo proteins displaying complex functional motifs. |
| Author | Corthésy, Patricia Yang, Che Eléouët, Jean-François Bates, John T Más, Vicente Kucharska, Iga Cramer, Johannes T Chiang, Chi-I Castoro, Giacomo Rameix-Welti, Marie-Anne Wen, Xiaolin Li, Yuxing Galloux, Marie Georgeon, Sandrine Richard, Charles-Adrien Jardetzky, Theodore Vollers, Sabrina S Oricchio, Elisa Descamps, Delphyne Julien, Jean-Philippe Krey, Thomas Bonet, Jaume Villard, Mélanie Wang, Yimeng Sesterhenn, Fabian Ervin, Sean Dheilly, Elie Riffault, Sabine Correia, Bruno E Delgado, Teresa Abriata, Luciano A Rosset, Stéphane |
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Yimeng orcidid: 0000-0003-0790-1277 surname: Wang fullname: Wang, Yimeng organization: Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD 20850, USA – sequence: 7 givenname: Chi-I surname: Chiang fullname: Chiang, Chi-I organization: Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD 20850, USA – sequence: 8 givenname: Luciano A orcidid: 0000-0003-3087-8677 surname: Abriata fullname: Abriata, Luciano A organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 9 givenname: Iga surname: Kucharska fullname: Kucharska, Iga organization: Departments of Biochemistry and Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada – sequence: 10 givenname: Giacomo surname: Castoro fullname: Castoro, Giacomo organization: Institute of Virology, Hannover Medical School, Hannover 30625, Germany – sequence: 11 givenname: Sabrina S orcidid: 0000-0002-6772-0155 surname: Vollers fullname: Vollers, Sabrina S organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 12 givenname: Marie surname: Galloux fullname: Galloux, Marie organization: Université Paris-Saclay, INRAE, UVSQ, VIM, 78350 Jouy-en-Josas, France – sequence: 13 givenname: Elie surname: Dheilly fullname: Dheilly, Elie organization: Swiss Institute for Experimental Cancer Research, School of Life Sciences, École Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland – sequence: 14 givenname: Stéphane orcidid: 0000-0002-8443-6017 surname: Rosset fullname: Rosset, Stéphane organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 15 givenname: Patricia surname: Corthésy fullname: Corthésy, Patricia organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 16 givenname: Sandrine orcidid: 0000-0002-8158-4508 surname: Georgeon fullname: Georgeon, Sandrine organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 17 givenname: Mélanie orcidid: 0000-0002-1306-4324 surname: Villard fullname: Villard, Mélanie organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland – sequence: 18 givenname: Charles-Adrien surname: Richard fullname: Richard, Charles-Adrien organization: Université Paris-Saclay, INRAE, UVSQ, VIM, 78350 Jouy-en-Josas, France – sequence: 19 givenname: Delphyne orcidid: 0000-0002-4883-6910 surname: Descamps fullname: Descamps, Delphyne organization: Université Paris-Saclay, INRAE, UVSQ, VIM, 78350 Jouy-en-Josas, France – sequence: 20 givenname: Teresa surname: Delgado fullname: Delgado, Teresa organization: Centro Nacional de Microbiología, Instituto de Salud Carlos III, 28220 Madrid, Spain – sequence: 21 givenname: Elisa orcidid: 0000-0002-1690-0447 surname: Oricchio fullname: Oricchio, Elisa organization: Swiss Institute for Experimental Cancer Research, School of Life Sciences, École Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland – sequence: 22 givenname: Marie-Anne orcidid: 0000-0002-5901-3856 surname: Rameix-Welti fullname: Rameix-Welti, Marie-Anne organization: UMR1173, INSERM, Université de Versailles St. Quentin, 78180 Montigny le Bretonneux, France – sequence: 23 givenname: Vicente surname: Más fullname: Más, Vicente organization: Centro Nacional de Microbiología, Instituto de Salud Carlos III, 28220 Madrid, Spain – sequence: 24 givenname: Sean orcidid: 0000-0001-8433-5382 surname: Ervin fullname: Ervin, Sean organization: Wake Forest Baptist Medical Center, Winston Salem, NC 27157, USA – sequence: 25 givenname: Jean-François orcidid: 0000-0002-7361-4885 surname: Eléouët fullname: Eléouët, Jean-François organization: Université Paris-Saclay, INRAE, UVSQ, VIM, 78350 Jouy-en-Josas, France – sequence: 26 givenname: Sabine surname: Riffault fullname: Riffault, Sabine organization: Université Paris-Saclay, INRAE, UVSQ, VIM, 78350 Jouy-en-Josas, France – sequence: 27 givenname: John T orcidid: 0000-0001-5545-6871 surname: Bates fullname: Bates, John T organization: University of Mississippi Medical Center, Jackson, MS 39216, USA – sequence: 28 givenname: Jean-Philippe orcidid: 0000-0001-7602-3995 surname: Julien fullname: Julien, Jean-Philippe organization: Departments of Biochemistry and Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada – sequence: 29 givenname: Yuxing surname: Li fullname: Li, Yuxing organization: Department of Microbiology and Immunology & Center of Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA – sequence: 30 givenname: Theodore orcidid: 0000-0002-3664-0072 surname: Jardetzky fullname: Jardetzky, Theodore organization: Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 31 givenname: Thomas orcidid: 0000-0002-4548-7241 surname: Krey fullname: Krey, Thomas organization: Centre for Structural Systems Biology (CSSB), 22607 Hamburg, Germany – sequence: 32 givenname: Bruno E orcidid: 0000-0002-7377-8636 surname: Correia fullname: Correia, Bruno E email: bruno.correia@epfl.ch organization: Swiss Institute of Bioinformatics (SIB), Lausanne CH-1015, Switzerland |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32409444$$D View this record in MEDLINE/PubMed |
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| PublicationTitle | IDEAS Working Paper Series from RePEc |
| PublicationTitleAlternate | Science |
| PublicationYear | 2020 |
| Publisher | Federal Reserve Bank of St. Louis |
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| References | 33674794 - Nat Methods. 2021 Mar;18(3):233. doi: 10.1038/s41592-021-01097-4 |
| References_xml | – reference: 33674794 - Nat Methods. 2021 Mar;18(3):233. doi: 10.1038/s41592-021-01097-4 |
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| Snippet | De novo protein design has been successful in expanding the natural protein repertoire. However, most de novo proteins lack biological function, presenting a... |
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| SubjectTerms | Amino Acid Motifs Antibodies, Neutralizing - biosynthesis Computational Biology - methods Humans Immunodominant Epitopes - chemistry Immunodominant Epitopes - immunology Protein Conformation Protein Engineering - methods Proteins Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - immunology Respiratory Syncytial Virus Vaccines - chemistry Respiratory Syncytial Virus Vaccines - immunology Respiratory Syncytial Virus, Human - immunology Single-Domain Antibodies - chemistry Single-Domain Antibodies - immunology Vaccines |
| Title | De novo protein design enables the precise induction of RSV-neutralizing antibodies |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/32409444 https://www.proquest.com/docview/2586569032 https://www.proquest.com/docview/2404046282 |
| Volume | 368 |
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