A SARS–CoV-2 Spike Receptor Binding Motif Peptide Induces Anti-Spike Antibodies in Mice andIs Recognized by COVID-19 Patients
The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer lea...
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| Published in | Frontiers in immunology Vol. 13; p. 879946 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Frontiers
26.05.2022
Frontiers Media S.A |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1664-3224 1664-3224 |
| DOI | 10.3389/fimmu.2022.879946 |
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| Abstract | The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM
436-507
) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM
436-507
synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. |
|---|---|
| AbstractList | The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM
436-507
) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM
436-507
synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM436-507) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM436-507 synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM ) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM436-507) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM436-507 synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production.The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM436-507) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM436-507 synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. The currently devastating pandemic of severe acute respiratory syndrome known as coronavirus disease 2019 or COVID-19 is caused by the coronavirus SARS-CoV-2. Both the virus and the disease have been extensively studied worldwide. A trimeric spike (S) protein expressed on the virus outer bilayer leaflet has been identified as a ligand that allows the virus to penetrate human host cells and cause infection. Its receptor-binding domain (RBD) interacts with the angiotensin-converting enzyme 2 (ACE2), the host-cell viral receptor, and is, therefore, the subject of intense research for the development of virus control means, particularly vaccines. In this work, we search for smaller fragments of the S protein able to elicit virus-neutralizing antibodies, suitable for production by peptide synthesis technology. Based on the analysis of available data, we selected a 72 aa long receptor binding motif (RBM 436-507 ) of RBD. We used ELISA to study the antibody response to each of the three antigens (S protein, its RBD domain and the RBM 436-507 synthetic peptide) in humans exposed to the infection and in immunized mice. The seroreactivity analysis showed that anti-RBM antibodies are produced in COVID-19 patients and immunized mice and may exert neutralizing function, although with a frequency lower than anti-S and -RBD. These results provide a basis for further studies towards the development of vaccines or treatments focused on specific regions of the S virus protein, which can benefit from the absence of folding problems, conformational constraints and other advantages of the peptide synthesis production. |
| Author | Kajava, Andrey V. Migliorini, Paola Rovero, Paolo Herrera, Sócrates Pratesi, Federico Quiceno, Sebastian Pacini, Lorenzo Peña-Moreno, Irina Charlot Corradin, Giampietro Arévalo-Herrera, Myriam Balam, Saidou Papini, Anna M. Carotenuto, Alfonso Diakité, Mahamadou M. Konaté, Drissa Errante, Fosca |
| AuthorAffiliation | 3 Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Department of Chemistry “Ugo Schiff”, University of Florence , Sesto Fiorentino , Italy 7 Department of Nephrology, University Hospital Regensburg , Regensburg , Germany 4 Department of Immunology, Caucaseco Scientific Research Center , Cali , Colombia 8 Department of Immunology, Malaria Vaccine and Drug Development Center , Cali , Colombia 6 Immunogenetic Laboratory and Parasitology, University of Sciences, Techniques and Technologies of Bamako (USTTB) , Bamako , Mali 5 Department of Pharmacy, University of Naples Federico II , Naples , Italy 10 Biochemistry Department, University of Lausanne , Lausanne , Switzerland 2 Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Department of NeuroFarBa, University of Florence , Sesto Fiorentino , Italy 9 CRBM, University of Montpellier, CNRS , Montpellier , France 1 Department of Clinical and Experimental Medicine, University Hospital of Pisa , Pisa , I |
| AuthorAffiliation_xml | – name: 3 Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Department of Chemistry “Ugo Schiff”, University of Florence , Sesto Fiorentino , Italy – name: 7 Department of Nephrology, University Hospital Regensburg , Regensburg , Germany – name: 9 CRBM, University of Montpellier, CNRS , Montpellier , France – name: 5 Department of Pharmacy, University of Naples Federico II , Naples , Italy – name: 4 Department of Immunology, Caucaseco Scientific Research Center , Cali , Colombia – name: 8 Department of Immunology, Malaria Vaccine and Drug Development Center , Cali , Colombia – name: 6 Immunogenetic Laboratory and Parasitology, University of Sciences, Techniques and Technologies of Bamako (USTTB) , Bamako , Mali – name: 2 Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Department of NeuroFarBa, University of Florence , Sesto Fiorentino , Italy – name: 1 Department of Clinical and Experimental Medicine, University Hospital of Pisa , Pisa , Italy – name: 10 Biochemistry Department, University of Lausanne , Lausanne , Switzerland |
| Author_xml | – sequence: 1 givenname: Federico surname: Pratesi fullname: Pratesi, Federico – sequence: 2 givenname: Fosca surname: Errante fullname: Errante, Fosca – sequence: 3 givenname: Lorenzo surname: Pacini fullname: Pacini, Lorenzo – sequence: 4 givenname: Irina Charlot surname: Peña-Moreno fullname: Peña-Moreno, Irina Charlot – sequence: 5 givenname: Sebastian surname: Quiceno fullname: Quiceno, Sebastian – sequence: 6 givenname: Alfonso surname: Carotenuto fullname: Carotenuto, Alfonso – sequence: 7 givenname: Saidou surname: Balam fullname: Balam, Saidou – sequence: 8 givenname: Drissa surname: Konaté fullname: Konaté, Drissa – sequence: 9 givenname: Mahamadou M. surname: Diakité fullname: Diakité, Mahamadou M. – sequence: 10 givenname: Myriam surname: Arévalo-Herrera fullname: Arévalo-Herrera, Myriam – sequence: 11 givenname: Andrey V. surname: Kajava fullname: Kajava, Andrey V. – sequence: 12 givenname: Paolo surname: Rovero fullname: Rovero, Paolo – sequence: 13 givenname: Giampietro surname: Corradin fullname: Corradin, Giampietro – sequence: 14 givenname: Paola surname: Migliorini fullname: Migliorini, Paola – sequence: 15 givenname: Anna M. surname: Papini fullname: Papini, Anna M. – sequence: 16 givenname: Sócrates surname: Herrera fullname: Herrera, Sócrates |
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| Copyright | Copyright © 2022 Pratesi, Errante, Pacini, Peña-Moreno, Quiceno, Carotenuto, Balam, Konaté, Diakité, Arévalo-Herrera, Kajava, Rovero, Corradin, Migliorini, Papini and Herrera. Distributed under a Creative Commons Attribution 4.0 International License Copyright © 2022 Pratesi, Errante, Pacini, Peña-Moreno, Quiceno, Carotenuto, Balam, Konaté, Diakité, Arévalo-Herrera, Kajava, Rovero, Corradin, Migliorini, Papini and Herrera 2022 Pratesi, Errante, Pacini, Peña-Moreno, Quiceno, Carotenuto, Balam, Konaté, Diakité, Arévalo-Herrera, Kajava, Rovero, Corradin, Migliorini, Papini and Herrera |
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| Keywords | COVID-19 SARS-CoV-2 receptor binding motif neutralizing Abs spike (S) protein immunized animals |
| Language | English |
| License | Copyright © 2022 Pratesi, Errante, Pacini, Peña-Moreno, Quiceno, Carotenuto, Balam, Konaté, Diakité, Arévalo-Herrera, Kajava, Rovero, Corradin, Migliorini, Papini and Herrera. Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Reviewed by: Nikhil Maroli, Indian Institute of Science (IISc), India; R. S. Rajmani, Indian Institute of Science (IISc), India These authors have contributed equally to this work This article was submitted to Vaccines and Molecular Therapeutics, a section of the journal Frontiers in Immunology Edited by: Pedro A. Reche, Complutense University of Madrid, Spain |
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| Title | A SARS–CoV-2 Spike Receptor Binding Motif Peptide Induces Anti-Spike Antibodies in Mice andIs Recognized by COVID-19 Patients |
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