Secondary Structures of MERS-CoV, SARS-CoV, and SARS-CoV-2 Spike Proteins Revealed by Infrared Vibrational Spectroscopy-Reference-Cited by-同舟云学术

Secondary Structures of MERS-CoV, SARS-CoV, and SARS-CoV-2 Spike Proteins Revealed by Infrared Vibrational Spectroscopy

Published:2023-05-31 Issue:11 Volume:24 Page:9550
ISSN:1422-0067
Container-title:International Journal of Molecular Sciences
language:en
Short-container-title:IJMS

Author:

D’Arco Annalisa¹²^ORCID,Di Fabrizio Marta³,Mancini Tiziana²^ORCID,Mosetti Rosanna²^ORCID,Macis Salvatore²,Tranfo Giovanna⁴^ORCID,Della Ventura Giancarlo¹⁵^ORCID,Marcelli Augusto¹⁶^ORCID,Petrarca Massimo⁷⁸^ORCID,Lupi Stefano²⁷

Affiliation:

1. Laboratori Nazionali Frascati, National Institute for Nuclear Physics (INFN-LNF), Via E. Fermi 54, 00044 Frascati, Italy

2. Department of Physics, University of Rome ‘La Sapienza’, P.le A. Moro 2, 00185 Rome, Italy

3. Laboratory of Biological Electron Microscopy, School of Basic Sciences, Institute of Physics, EPFL & Department of Fundamental Microbiology, Faculty of Biology and Medicine, UNIL, 1015 Lausanne, Switzerland

4. Department of Occupational and Environmental Medicine, Epidemiology and Hygiene, INAIL, Monte Porzio Catone, 00078 Rome, Italy

5. Department of Science, University Rome Tre, Largo San Leonardo Murialdo 1, 00146 Rome, Italy

6. Rome International Centre for Materials Science Superstipes, Via dei Sabelli 119A, 00185 Rome, Italy

7. National Institute for Nuclear Physics Section Rome1, P.le A. Moro 2, 00185 Rome, Italy

8. Department of Basic and Applied Sciences for Engineering (SBAI), University of Rome ’La Sapienza’, Via Scarpa 16, 00161 Rome, Italy

Abstract

All coronaviruses are characterized by spike glycoproteins whose S1 subunits contain the receptor binding domain (RBD). The RBD anchors the virus to the host cellular membrane to regulate the virus transmissibility and infectious process. Although the protein/receptor interaction mainly depends on the spike’s conformation, particularly on its S1 unit, their secondary structures are poorly known. In this paper, the S1 conformation was investigated for MERS-CoV, SARS-CoV, and SARS-CoV-2 at serological pH by measuring their Amide I infrared absorption bands. The SARS-CoV-2 S1 secondary structure revealed a strong difference compared to those of MERS-CoV and SARS-CoV, with a significant presence of extended β-sheets. Furthermore, the conformation of the SARS-CoV-2 S1 showed a significant change by moving from serological pH to mild acidic and alkaline pH conditions. Both results suggest the capability of infrared spectroscopy to follow the secondary structure adaptation of the SARS-CoV-2 S1 to different environments.

Publisher

MDPI AG

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis

Link

https://www.mdpi.com/1422-0067/24/11/9550/pdf

Reference73 articles.

1. Early Transmission Dynamics in Wuhan, China, of Novel Coronavirus-Infected Pneumonia;Li;N. Engl. J. Med.,2020

2. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China;Huang;Lancet,2020

3. Structural and functional properties of SARS-CoV-2 spike protein: Potential antivirus drug development for COVID-19;Huang;Acta Pharmacol. Sin.,2020

4. A Novel Coronavirus from Patients with Pneumonia in China;Zhu;N. Engl. J. Med.,2019

5. Identification of a novel coronavirus in patients with severe acute respiratory syndrome;Drosten;N. Engl. J. Med.,2003