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Updated: Oct 9, 2025
Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Active site-based analysis of structural proteins for drug targets in different human Coronaviruses
Khadijeh Ahmadi1, Farnaz Zahedifard2, Ladan Mafakher3
1Infectious and Tropical Diseases Research Center, Hormozgan Health Institute, Hormozgan University of Medical Sciences, Bandar Abbas, Iran.
Abstract:
Seven types of Coronaviruses (CoVs) have been identified that can cause infection in humans, including HCoV-229E, HCoV-NL63, HCoV-OC43, HCoV-HKU1, SARS-CoV, HCoV-MERS, and SARS-CoV-2. In this study, we investigated the genetic structure, the homology of the structural protein sequences, as well as the investigation of the active site of structural proteins. The active site of structural proteins was determined based on the previous studies, and the homology of their amino acid sequences and structure was compared. Multiple sequence alignment of Spike protein of HCoVs showed that the receptor-binding domain of SARS-CoV-2, SARS-CoV, and MERS-CoV was located at a similar site to the S1 subunit. The binding motif of PDZ (postsynaptic density-95/disks large/zona occludens-1) of the envelope protein, was conserved in SARS-CoV and SARS-CoV-2 according to multiple sequence alignment but showed different changes in the other HCoVs. Overall, spike protein showed the most variation in its active sites, but the other structural proteins were highly conserved. In this study, for the first time, the active site of all structural proteins of HCoVs as a drug target was investigated. The binding site of these proteins can be suitable targets for drugs or vaccines among HCoVs.
Insights
This study analyzed structural proteins of seven human Coronaviruses (CoVs). Spike proteins varied most, while others were conserved, suggesting potential drug and vaccine targets.
Area of Science:
- Virology
- Structural Biology
- Drug Discovery
Background:
- Seven types of Coronaviruses (CoVs) cause human infections.
- Understanding CoV structural protein homology is crucial for therapeutic development.
Purpose of the Study:
- Investigate the genetic structure and protein sequence homology of human CoVs.
- Identify conserved and variable regions within structural proteins for drug and vaccine targeting.
Main Methods:
- Comparative analysis of structural protein sequences and active sites across seven human CoVs.
- Multiple sequence alignment of Spike (S) protein and Envelope (E) protein.
- Identification of conserved binding motifs, including PDZ domains.
Main Results:
- Spike protein exhibited the most variation in active sites among human CoVs.
- Receptor-binding domains of SARS-CoV-2, SARS-CoV, and MERS-CoV are similarly located.
- PDZ binding motifs in the envelope protein were conserved in SARS-CoV and SARS-CoV-2.
Conclusions:
- Structural proteins of human CoVs, particularly the spike protein, present diverse active sites.
- Conserved structural proteins offer potential targets for broad-spectrum antiviral drugs and vaccines against Coronaviruses.
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