ACE2-binding exposes the SARS-CoV-2 fusion peptide to broadly neutralizing coronavirus antibodies

The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immu...

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Published inScience (American Association for the Advancement of Science) Vol. 377; no. 6607; pp. 735 - 742
Main Authors Low, Jun Siong, Jerak, Josipa, Tortorici, M. Alejandra, McCallum, Matthew, Pinto, Dora, Cassotta, Antonino, Foglierini, Mathilde, Mele, Federico, Abdelnabi, Rana, Weynand, Birgit, Noack, Julia, Montiel-Ruiz, Martin, Bianchi, Siro, Benigni, Fabio, Sprugasci, Nicole, Joshi, Anshu, Bowen, John E., Stewart, Cameron, Rexhepaj, Megi, Walls, Alexandra C., Jarrossay, David, Morone, Diego, Paparoditis, Philipp, Garzoni, Christian, Ferrari, Paolo, Ceschi, Alessandro, Neyts, Johan, Purcell, Lisa A., Snell, Gyorgy, Corti, Davide, Lanzavecchia, Antonio, Veesler, David, Sallusto, Federica
Format Journal Article
LanguageEnglish
Published United States American Association for the Advancement of Science 12.08.2022
Subjects
Angiotensin-Converting Enzyme 2 - chemistry
Animals
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - isolation & purification
Antibodies, Viral - immunology
Antibodies, Viral - isolation & purification
Biochem
Broadly Neutralizing Antibodies - immunology
COVID-19 - immunology
Humans
Microbio
Peptides - immunology
Protein Binding
SARS-CoV-2 - immunology
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - immunology
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Abstract The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide–specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs. Seven coronaviruses cause human disease, and three have caused serious outbreaks in the past 20 years. The potential for future coronavirus outbreaks in humans and the ongoing resistance of severe acute syndrome coronavirus 2 (SARS-CoV-2) variants to existing antibodies make it important to identify cross-reactive antibodies that can be the basis of therapeutics and can guide vaccine design. Low et al . and Dacon et al . isolated antibodies from convalescent individuals that show broad neutralizing activity against a range of coronaviruses, including Omicron variants of SARS-CoV-2. The antibodies target a conserved region of the viral spike protein known as the fusion peptide and may act by preventing the cell fusion that is required for infection of new host cells. —VV A class of broadly reactive antibodies target a cryptic fusion peptide epitope exposed upon coronavirus spike protein binding to ACE2.
AbstractList The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide-specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs.
The coronavirus spike (S) glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus S proteins. This class of mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and beta-coronaviruses, including animal coronavirus WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses show that the fusion peptide-specific mAbs bind with different modalities to a cryptic epitope, which is hidden in prefusion stabilized S, and becomes exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs.
The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide–specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs. Seven coronaviruses cause human disease, and three have caused serious outbreaks in the past 20 years. The potential for future coronavirus outbreaks in humans and the ongoing resistance of severe acute syndrome coronavirus 2 (SARS-CoV-2) variants to existing antibodies make it important to identify cross-reactive antibodies that can be the basis of therapeutics and can guide vaccine design. Low et al . and Dacon et al . isolated antibodies from convalescent individuals that show broad neutralizing activity against a range of coronaviruses, including Omicron variants of SARS-CoV-2. The antibodies target a conserved region of the viral spike protein known as the fusion peptide and may act by preventing the cell fusion that is required for infection of new host cells. —VV A class of broadly reactive antibodies target a cryptic fusion peptide epitope exposed upon coronavirus spike protein binding to ACE2.
The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide-specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs.The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide-specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs.
Author Snell, Gyorgy
Lanzavecchia, Antonio
Montiel-Ruiz, Martin
Veesler, David
Walls, Alexandra C.
Jerak, Josipa
Tortorici, M. Alejandra
Bianchi, Siro
Sprugasci, Nicole
Joshi, Anshu
Bowen, John E.
Rexhepaj, Megi
Benigni, Fabio
Sallusto, Federica
Noack, Julia
Neyts, Johan
Ceschi, Alessandro
Stewart, Cameron
Foglierini, Mathilde
Abdelnabi, Rana
Paparoditis, Philipp
Ferrari, Paolo
Morone, Diego
McCallum, Matthew
Pinto, Dora
Jarrossay, David
Weynand, Birgit
Cassotta, Antonino
Corti, Davide
Purcell, Lisa A.
Garzoni, Christian
Low, Jun Siong
Mele, Federico
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/35857703$$D View this record in MEDLINE/PubMed
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Snippet The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal...
The coronavirus spike (S) glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated from severe acute...
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StartPage 735
SubjectTerms Angiotensin-Converting Enzyme 2 - chemistry
Animals
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - isolation & purification
Antibodies, Viral - immunology
Antibodies, Viral - isolation & purification
Biochem
Broadly Neutralizing Antibodies - immunology
COVID-19 - immunology
Humans
Microbio
Peptides - immunology
Protein Binding
SARS-CoV-2 - immunology
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - immunology
Title ACE2-binding exposes the SARS-CoV-2 fusion peptide to broadly neutralizing coronavirus antibodies
URI https://www.ncbi.nlm.nih.gov/pubmed/35857703
https://www.proquest.com/docview/2692072791
https://pubmed.ncbi.nlm.nih.gov/PMC9348755
Volume 377
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