Pan-ebolavirus protective therapy by two multifunctional human antibodies
Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important...
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| Published in | Cell Vol. 184; no. 22; pp. 5593 - 5607.e18 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
28.10.2021
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy.
[Display omitted]
•Two human antibodies recognize different conserved sites on ebolavirus glycoproteins•The cocktail exhibits broad neutralizing activity and resists viral escape in vitro•Antibodies synergize to neutralize virus and differentially engage their Fc regions•The therapeutic cocktail protects NHPs against three medically important ebolaviruses
A broad-spectrum therapeutic antibody treatment against medically important ebolaviruses is not available but highly desirable. Gilchuk et al. report a therapeutic cocktail comprising two broadly neutralizing human antibodies that exhibit synergistic neutralizing activity, complementary Fc region-mediated effector functions, resistance to viral escape, and protection of non-human primates from disease caused by Ebola, Bundibugyo, or Sudan ebolaviruses with high effectiveness and also define the structural basis for neutralization breadth and potency by this cocktail. |
|---|---|
| AbstractList | A broad-spectrum therapeutic antibody treatment against medically important ebolaviruses is not available but highly desirable. Gilchuk
et al
. report a therapeutic cocktail comprising two broadly-neutralizing human antibodies that exhibit synergistic neutralizing activity, complementary Fc region-mediated effector functions, resistance to viral escape, and protection of non-human primates from disease caused by Ebola, Bundibugyo, or Sudan ebolaviruses with high effectiveness, and also define the structural basis for neutralization breadth and potency by this cocktail.
Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies rEBOV-515 and rEBOV-442 that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal
in vivo
activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy. Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy. Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy.Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy. Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy. Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available recently have a narrow therapeutic spectrum and are ineffective against ebolaviruses other than Ebola virus (EBOV), including medically important Bundibugyo (BDBV) and Sudan (SUDV) viruses. Here, we report the development of a therapeutic cocktail comprising two broadly neutralizing human antibodies, rEBOV-515 and rEBOV-442, that recognize non-overlapping sites on the ebolavirus glycoprotein (GP). Antibodies in the cocktail exhibited synergistic neutralizing activity, resisted viral escape, and possessed differing requirements for their Fc-regions for optimal in vivo activities. The cocktail protected non-human primates from ebolavirus disease caused by EBOV, BDBV, or SUDV with high therapeutic effectiveness. High-resolution structures of the cocktail antibodies in complex with GP revealed the molecular determinants for neutralization breadth and potency. This study provides advanced preclinical data to support clinical development of this cocktail for pan-ebolavirus therapy. [Display omitted] •Two human antibodies recognize different conserved sites on ebolavirus glycoproteins•The cocktail exhibits broad neutralizing activity and resists viral escape in vitro•Antibodies synergize to neutralize virus and differentially engage their Fc regions•The therapeutic cocktail protects NHPs against three medically important ebolaviruses A broad-spectrum therapeutic antibody treatment against medically important ebolaviruses is not available but highly desirable. Gilchuk et al. report a therapeutic cocktail comprising two broadly neutralizing human antibodies that exhibit synergistic neutralizing activity, complementary Fc region-mediated effector functions, resistance to viral escape, and protection of non-human primates from disease caused by Ebola, Bundibugyo, or Sudan ebolaviruses with high effectiveness and also define the structural basis for neutralization breadth and potency by this cocktail. |
| Author | Zost, Seth J. Murin, Charles D. Borisevich, Viktoriya Bombardi, Robin G. Ilinykh, Philipp A. Nargi, Rachel S. Carnahan, Robert H. Geisbert, Joan B. Suryadevara, Naveenchandra Kuzmina, Natalia Gilchuk, Pavlo Agans, Krystle N. Sutton, Rachel E. Crowe, James E. Geisbert, Thomas W. Cross, Robert W. Bukreyev, Alexander Ward, Andrew B. Huang, Kai |
| AuthorAffiliation | 7 Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN, 37232, USA 1 Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN, 37232, USA 3 Galveston National Laboratory, Galveston, TX, 77550, USA 5 Department of Pathology, University of Texas Medical Branch, Galveston, TX, 77555, USA 6 Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, 37232, USA 2 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA 4 Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, TX, 77555, USA |
| AuthorAffiliation_xml | – name: 3 Galveston National Laboratory, Galveston, TX, 77550, USA – name: 5 Department of Pathology, University of Texas Medical Branch, Galveston, TX, 77555, USA – name: 2 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA – name: 1 Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN, 37232, USA – name: 4 Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, TX, 77555, USA – name: 6 Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, 37232, USA – name: 7 Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN, 37232, USA |
| Author_xml | – sequence: 1 givenname: Pavlo surname: Gilchuk fullname: Gilchuk, Pavlo organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 2 givenname: Charles D. surname: Murin fullname: Murin, Charles D. organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 3 givenname: Robert W. surname: Cross fullname: Cross, Robert W. organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 4 givenname: Philipp A. surname: Ilinykh fullname: Ilinykh, Philipp A. organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 5 givenname: Kai surname: Huang fullname: Huang, Kai organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 6 givenname: Natalia surname: Kuzmina fullname: Kuzmina, Natalia organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 7 givenname: Viktoriya surname: Borisevich fullname: Borisevich, Viktoriya organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 8 givenname: Krystle N. surname: Agans fullname: Agans, Krystle N. organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 9 givenname: Joan B. surname: Geisbert fullname: Geisbert, Joan B. organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 10 givenname: Seth J. surname: Zost fullname: Zost, Seth J. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 11 givenname: Rachel S. surname: Nargi fullname: Nargi, Rachel S. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 12 givenname: Rachel E. surname: Sutton fullname: Sutton, Rachel E. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 13 givenname: Naveenchandra surname: Suryadevara fullname: Suryadevara, Naveenchandra organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 14 givenname: Robin G. surname: Bombardi fullname: Bombardi, Robin G. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 15 givenname: Robert H. surname: Carnahan fullname: Carnahan, Robert H. organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 16 givenname: Alexander surname: Bukreyev fullname: Bukreyev, Alexander organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 17 givenname: Thomas W. surname: Geisbert fullname: Geisbert, Thomas W. organization: Galveston National Laboratory, Galveston, TX 77550, USA – sequence: 18 givenname: Andrew B. surname: Ward fullname: Ward, Andrew B. organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 19 givenname: James E. surname: Crowe fullname: Crowe, James E. email: james.crowe@vumc.org organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34715022$$D View this record in MEDLINE/PubMed |
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| Keywords | antibody therapeutics Ebolavirus neutralizing antibodies glycoprotein ebolavirus infection viral antibodies epitope mapping |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Senior author. These authors contributed equally. AUTHOR CONTRIBUTIONS P.G., C.D.M., R.W.C., R.C., A.B., T.W.G., A.B.W., and J.E.C. planned the studies. P.G., C.D.M., R.W.C., P.A.I., K.H., V.B., K.N.A., J.B.G., N.K., T.A., R.S.N., R.E.S., N.S., S.J.Z., and R.G.B. conducted experiments. P.G., C.D.M., R.W.C., A.B., T.W.G., A.B.W., and J.E.C. interpreted the studies. P.G., C.D.M., and J.E.C. wrote the first draft of the paper. A.B., T.W.G., A.B.W, and J.E.C. obtained funding. All authors reviewed, edited and approved the paper. |
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Natl. Acad. Sci. USA doi: 10.1073/pnas.1914985117 |
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| Snippet | Ebolaviruses cause a severe and often fatal illness with the potential for global spread. Monoclonal antibody-based treatments that have become available... A broad-spectrum therapeutic antibody treatment against medically important ebolaviruses is not available but highly desirable. Gilchuk et al . report a... |
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| SubjectTerms | Amino Acid Sequence Animals Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antibodies, Viral - immunology antibody therapeutics Binding Sites Cell Line Cryoelectron Microscopy Ebolavirus Ebolavirus - immunology Ebolavirus - ultrastructure ebolavirus infection epitope mapping Epitopes - immunology Female glycoprotein glycoproteins Glycoproteins - chemistry Glycoproteins - immunology Hemorrhagic Fever, Ebola - immunology Hemorrhagic Fever, Ebola - prevention & control Hemorrhagic Fever, Ebola - virology Humans Hydrogen-Ion Concentration Mice Mice, Inbred BALB C Models, Molecular neutralization neutralizing antibodies Primates Receptors, Fc - metabolism Recombinant Proteins - immunology Sudan therapeutics viral antibodies Viremia - immunology |
| Title | Pan-ebolavirus protective therapy by two multifunctional human antibodies |
| URI | https://dx.doi.org/10.1016/j.cell.2021.09.035 https://www.ncbi.nlm.nih.gov/pubmed/34715022 https://www.proquest.com/docview/2590137195 https://www.proquest.com/docview/2636621572 https://pubmed.ncbi.nlm.nih.gov/PMC8716180 |
| Volume | 184 |
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