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.

A SARS–CoV-2 Spike Receptor Binding Motif Peptide Induces Anti-Spike Antibodies in Mice andIs Recognized by COVID-19 Patients / Pratesi, Federico; Errante, Fosca; Pacini, Lorenzo; Peña-Moreno, Irina Charlot; Quiceno, Sebastian; Carotenuto, Alfonso; Balam, Saidou; Konaté, Drissa; Diakité, Mahamadou M.; Arévalo-Herrera, Myriam; Kajava, Andrey V.; Rovero, Paolo; Corradin, Giampietro; Migliorini, Paola; Papini, Anna M.; Herrera, Sócrates. - In: FRONTIERS IN IMMUNOLOGY. - ISSN 1664-3224. - ELETTRONICO. - 13:(2022), pp. 1-11. [10.3389/fimmu.2022.879946]

A SARS–CoV-2 Spike Receptor Binding Motif Peptide Induces Anti-Spike Antibodies in Mice andIs Recognized by COVID-19 Patients

Errante, Fosca;Pacini, Lorenzo;Rovero, Paolo;Papini, Anna M.;
2022

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 (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.
2022
13
1
11
Goal 3: Good health and well-being for people
Pratesi, Federico; Errante, Fosca; Pacini, Lorenzo; Peña-Moreno, Irina Charlot; Quiceno, Sebastian; Carotenuto, Alfonso; Balam, Saidou; Konaté, Drissa; Diakité, Mahamadou M.; Arévalo-Herrera, Myriam; Kajava, Andrey V.; Rovero, Paolo; Corradin, Giampietro; Migliorini, Paola; Papini, Anna M.; Herrera, Sócrates
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1270584
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