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Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2.
Cells. 2020 12 08; 9(12)C

Abstract

The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has recently emerged in China and caused a disease called coronavirus disease 2019 (COVID-19). The virus quickly spread around the world, causing a sustained global outbreak. Although SARS-CoV-2, and other coronaviruses, SARS-CoV and Middle East respiratory syndrome CoV (MERS-CoV) are highly similar genetically and at the protein production level, there are significant differences between them. Research has shown that the structural spike (S) protein plays an important role in the evolution and transmission of SARS-CoV-2. So far, studies have shown that various genes encoding primarily for elements of S protein undergo frequent mutation. We have performed an in-depth review of the literature covering the structural and mutational aspects of S protein in the context of SARS-CoV-2, and compared them with those of SARS-CoV and MERS-CoV. Our analytical approach consisted in an initial genome and transcriptome analysis, followed by primary, secondary and tertiary protein structure analysis. Additionally, we investigated the potential effects of these differences on the S protein binding and interactions to angiotensin-converting enzyme 2 (ACE2), and we established, after extensive analysis of previous research articles, that SARS-CoV-2 and SARS-CoV use different ends/regions in S protein receptor-binding motif (RBM) and different types of interactions for their chief binding with ACE2. These differences may have significant implications on pathogenesis, entry and ability to infect intermediate hosts for these coronaviruses. This review comprehensively addresses in detail the variations in S protein, its receptor-binding characteristics and detailed structural interactions, the process of cleavage involved in priming, as well as other differences between coronaviruses.

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Authors+Show Affiliations

Hatmal MM
Department of Medical Laboratory Sciences, Faculty of Applied Health Sciences, The Hashemite University, Zarqa 13133, Jordan.
Alshaer W
Cell Therapy Center (CTC), The University of Jordan, Amman 11942, Jordan.
Al-Hatamleh MAI
Department of Immunology, School of Medical Sciences, Universiti Sains Malaysia, Kubang Kerian, Kelantan 16150, Malaysia.
Hatmal M
Prince Hamza Hospital, Amman 11947, Jordan.
Smadi O
Department of Biomedical Engineering, Faculty of Engineering, The Hashemite University, Zarqa 13133, Jordan.
Taha MO
Drug Design and Discovery Unit, Department of Pharmaceutical Sciences, Faculty of Pharmacy, The University of Jordan, Amman 11942, Jordan.
Oweida AJ
Department of Nuclear Medicine and Radiobiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC J1H 5N4, Canada.
Boer JC
Translational Immunology and Nanotechnology Unit, School of Health and Biomedical Sciences, RMIT University, Bundoora 3083, Australia.
Mohamud R
Department of Immunology, School of Medical Sciences, Universiti Sains Malaysia, Kubang Kerian, Kelantan 16150, Malaysia. Hospital Universiti Sains Malaysia, Health Campus, Kubang Kerian, Kelantan 16150, Malaysia.
Plebanski M
Translational Immunology and Nanotechnology Unit, School of Health and Biomedical Sciences, RMIT University, Bundoora 3083, Australia.

MeSH

Angiotensin-Converting Enzyme 2Binding SitesCOVID-19HumansMiddle East Respiratory Syndrome CoronavirusMolecular Dynamics SimulationProtein Structure, TertiarySevere acute respiratory syndrome-related coronavirusSARS-CoV-2Spike Glycoprotein, Coronavirus

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

33302501

Citation

Hatmal, Ma'mon M., et al. "Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions With ACE2." Cells, vol. 9, no. 12, 2020.
Hatmal MM, Alshaer W, Al-Hatamleh MAI, et al. Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2. Cells. 2020;9(12).
Hatmal, M. M., Alshaer, W., Al-Hatamleh, M. A. I., Hatmal, M., Smadi, O., Taha, M. O., Oweida, A. J., Boer, J. C., Mohamud, R., & Plebanski, M. (2020). Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2. Cells, 9(12). https://doi.org/10.3390/cells9122638
Hatmal MM, et al. Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions With ACE2. Cells. 2020 12 8;9(12) PubMed PMID: 33302501.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2. AU - Hatmal,Ma'mon M, AU - Alshaer,Walhan, AU - Al-Hatamleh,Mohammad A I, AU - Hatmal,Malik, AU - Smadi,Othman, AU - Taha,Mutasem O, AU - Oweida,Ayman J, AU - Boer,Jennifer C, AU - Mohamud,Rohimah, AU - Plebanski,Magdalena, Y1 - 2020/12/08/ PY - 2020/10/31/received PY - 2020/12/01/revised PY - 2020/12/04/accepted PY - 2020/12/11/entrez PY - 2020/12/12/pubmed PY - 2020/12/17/medline KW - COVID-19 KW - coronaviruses KW - proline KW - receptor-binding motif KW - spike protein KW - terminal region JF - Cells JO - Cells VL - 9 IS - 12 N2 - The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has recently emerged in China and caused a disease called coronavirus disease 2019 (COVID-19). The virus quickly spread around the world, causing a sustained global outbreak. Although SARS-CoV-2, and other coronaviruses, SARS-CoV and Middle East respiratory syndrome CoV (MERS-CoV) are highly similar genetically and at the protein production level, there are significant differences between them. Research has shown that the structural spike (S) protein plays an important role in the evolution and transmission of SARS-CoV-2. So far, studies have shown that various genes encoding primarily for elements of S protein undergo frequent mutation. We have performed an in-depth review of the literature covering the structural and mutational aspects of S protein in the context of SARS-CoV-2, and compared them with those of SARS-CoV and MERS-CoV. Our analytical approach consisted in an initial genome and transcriptome analysis, followed by primary, secondary and tertiary protein structure analysis. Additionally, we investigated the potential effects of these differences on the S protein binding and interactions to angiotensin-converting enzyme 2 (ACE2), and we established, after extensive analysis of previous research articles, that SARS-CoV-2 and SARS-CoV use different ends/regions in S protein receptor-binding motif (RBM) and different types of interactions for their chief binding with ACE2. These differences may have significant implications on pathogenesis, entry and ability to infect intermediate hosts for these coronaviruses. This review comprehensively addresses in detail the variations in S protein, its receptor-binding characteristics and detailed structural interactions, the process of cleavage involved in priming, as well as other differences between coronaviruses. SN - 2073-4409 UR - https://www.unboundmedicine.com/medline/citation/33302501/Comprehensive_Structural_and_Molecular_Comparison_of_Spike_Proteins_of_SARS_CoV_2_SARS_CoV_and_MERS_CoV_and_Their_Interactions_with_ACE2_ DB - PRIME DP - Unbound Medicine ER -