ArticleInternational journal of molecular sciences2023
Secondary Structures of MERS-CoV, SARS-CoV, and SARS-CoV-2 Spike Proteins Revealed by Infrared Vibrational Spectroscopy.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Spectroscopic Insights into Lysozyme Structural Modulation by Polyphenols: A Combined FTIR and VCD Study.Molecules (Basel, Switzerland) · 2026Article
- A Combined Experimental-Theoretical Approach Unveils the Comprehensive Asn Deamidation Kinetics.Journal of the American Chemical Society · 2026Article
- Spectroscopic secondary structure fingerprint of β-variant of SARS-CoV-2 spike glycoprotein.European biophysics journal : EBJ · 2026Article
- In Silico Ligand-Based Screening of PDB Database for Searching Unique Motifs Against SARS-CoV-2.Biomolecules · 2026Article
- Thrombotic complications in critically ill patients with coronavirus infections: A comparative study of MERS and COVID-19.Medicine · 2025Observational
- Multimodal Structural Characterization of SARS-CoV-2 Spike Variants: Spectroscopic and Computational Insights.International journal of molecular sciences · 2025Article
- Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Nanofibrous Conductive Sensor for Limonene: One-Step Synthesis via Electrospinning and Molecular Imprinting.Nanomaterials (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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