Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-doma...
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| Published in | Cell Vol. 181; no. 5; pp. 1004 - 1015.e15 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
28.05.2020
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks.
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•VHHs isolated from a llama immunized with prefusion-stabilized coronavirus spikes•Structural characterization of VHHs reveals conserved mechanism of neutralization•SARS-CoV-1 S-directed VHH cross-reacts with SARS-CoV-2 S•Bivalent VHH neutralizes SARS-CoV-2 pseudoviruses
Using llamas immunized with prefusion-stabilized betacoronavirus spike proteins, Wrapp et al. identify neutralizing cross-reactive single-domain camelid antibodies, which may serve not only as useful reagents for researchers studying the viruses causing MERS, SARS, and COVID-19, but also potential therapeutic candidates. Crystal structures further reveal how these antibodies bind spike proteins to prevent virus entry into cells. |
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| AbstractList | Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks.Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. • VHHs isolated from a llama immunized with prefusion-stabilized coronavirus spikes • Structural characterization of VHHs reveals conserved mechanism of neutralization • SARS-CoV-1 S-directed VHH cross-reacts with SARS-CoV-2 S • Bivalent VHH neutralizes SARS-CoV-2 pseudoviruses Using llamas immunized with prefusion-stabilized betacoronavirus spike proteins, Wrapp et al. identify neutralizing cross-reactive single-domain camelid antibodies, which may serve not only as useful reagents for researchers studying the viruses causing MERS, SARS, and COVID-19, but also potential therapeutic candidates. Crystal structures further reveal how these antibodies bind spike proteins to prevent virus entry into cells. Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. [Display omitted] •VHHs isolated from a llama immunized with prefusion-stabilized coronavirus spikes•Structural characterization of VHHs reveals conserved mechanism of neutralization•SARS-CoV-1 S-directed VHH cross-reacts with SARS-CoV-2 S•Bivalent VHH neutralizes SARS-CoV-2 pseudoviruses Using llamas immunized with prefusion-stabilized betacoronavirus spike proteins, Wrapp et al. identify neutralizing cross-reactive single-domain camelid antibodies, which may serve not only as useful reagents for researchers studying the viruses causing MERS, SARS, and COVID-19, but also potential therapeutic candidates. Crystal structures further reveal how these antibodies bind spike proteins to prevent virus entry into cells. Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. |
| Author | Schepens, Bert Corbett, Kizzmekia S. Van Breedam, Wander Callewaert, Nico van Schie, Loes De Vlieger, Dorien Wang, Nianshuang Hoffmann, Markus Wrapp, Daniel Graham, Barney S. Saelens, Xavier Torres, Gretel M. McLellan, Jason S. Roose, Kenny Pöhlmann, Stefan |
| Author_xml | – sequence: 1 givenname: Daniel surname: Wrapp fullname: Wrapp, Daniel organization: Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 2 givenname: Dorien surname: De Vlieger fullname: De Vlieger, Dorien organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 3 givenname: Kizzmekia S. surname: Corbett fullname: Corbett, Kizzmekia S. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 4 givenname: Gretel M. surname: Torres fullname: Torres, Gretel M. organization: Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03756, USA – sequence: 5 givenname: Nianshuang surname: Wang fullname: Wang, Nianshuang organization: Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA – sequence: 6 givenname: Wander surname: Van Breedam fullname: Van Breedam, Wander organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 7 givenname: Kenny surname: Roose fullname: Roose, Kenny organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 8 givenname: Loes surname: van Schie fullname: van Schie, Loes organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 9 givenname: Markus surname: Hoffmann fullname: Hoffmann, Markus organization: Infection Biology Unit, German Primate Center – Leibniz Institute for Primate Research, 37077 Göttingen, Germany – sequence: 10 givenname: Stefan surname: Pöhlmann fullname: Pöhlmann, Stefan organization: Infection Biology Unit, German Primate Center – Leibniz Institute for Primate Research, 37077 Göttingen, Germany – sequence: 11 givenname: Barney S. surname: Graham fullname: Graham, Barney S. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 12 givenname: Nico surname: Callewaert fullname: Callewaert, Nico organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 13 givenname: Bert surname: Schepens fullname: Schepens, Bert email: bert.schepens@vib-ugent.be organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 14 givenname: Xavier surname: Saelens fullname: Saelens, Xavier email: xavier.saelens@vib-ugent.be organization: VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium – sequence: 15 givenname: Jason S. orcidid: 0000-0003-3991-542X surname: McLellan fullname: McLellan, Jason S. email: jmclellan@austin.utexas.edu organization: Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32375025$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Animals antibodies Antibodies, Neutralizing - chemistry Antibodies, Neutralizing - immunology Antibodies, Neutralizing - isolation & purification Betacoronavirus - immunology Camelidae Camelids, New World - immunology Coronavirus infections Coronavirus Infections - therapy COVID-19 cross reaction Cross Reactions crystal structure epitopes humans immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - immunology llamas membrane fusion MERS Middle East respiratory syndrome coronavirus Models, Molecular nanobody neutralization Pandemics Pneumonia, Viral - therapy Protein Domains receptors Receptors, Virus - chemistry SARS SARS-CoV-2 Single-Domain Antibodies - chemistry Single-Domain Antibodies - immunology Single-Domain Antibodies - isolation & purification Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - immunology therapeutics viruses |
| Title | Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies |
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