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SARS-Cov2 S Protein Features Potential Estrogen Binding Site

RESEARCH BACKGROUND: During the current SARS-CoV2 pandemic, as well as earlier SARS and MERS epidemics, it has been observed that COVID19-positive women on average tend to have milder symptoms and lower fatality rates than men. There is a number of differences between the sexes known to contribute t...

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Autores principales: Tomasović, Ante, Stanzer, Damir, Krešimir Svetec, Ivan, Svetec Miklenić, Marina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: University of Zagreb Faculty of Food Technology and Biotechnology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157085/
https://www.ncbi.nlm.nih.gov/pubmed/34084077
http://dx.doi.org/10.17113/ftb.59.01.21.6820
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author Tomasović, Ante
Stanzer, Damir
Krešimir Svetec, Ivan
Svetec Miklenić, Marina
author_facet Tomasović, Ante
Stanzer, Damir
Krešimir Svetec, Ivan
Svetec Miklenić, Marina
author_sort Tomasović, Ante
collection PubMed
description RESEARCH BACKGROUND: During the current SARS-CoV2 pandemic, as well as earlier SARS and MERS epidemics, it has been observed that COVID19-positive women on average tend to have milder symptoms and lower fatality rates than men. There is a number of differences between the sexes known to contribute to different immune responses and severity of the disease, one being the effect of estrogen via estrogen receptor signalling. We wondered if estrogen might also affect the SARS-CoV2 more directly, perhaps by binding to the surface glycoprotein (S protein), thus possibly reducing its infectivity. EXPERIMENTAL APPROACH: To assess whether there is a possibility for estrogen binding on the SARS-CoV2 S protein, we used BLAST and HHpred to compare protein sequences of S protein and human estrogen receptor β, while 3D structures of a potential estrogen binding site and an active site of estrogen receptor β were visualized and compared using PyMOL. RESULTS AND CONCLUSIONS: By comparing the sequence of SARS-CoV2 S protein with the human estrogen receptor β, we identified a potential estrogen binding site on S protein and further determined that it also shares notable similarities with the active site of ER β when observed in 3D structure of their respective proteins. As a control, SARS-CoV2 S protein was compared with the human androgen receptor, and no such similarities were found. The potential estrogen binding site is part of coronavirus S2 superfamily domain, which is involved in host-virus membrane fusion during infection and appears to be conserved throughout the Coronaviridae family. NOVELTY AND SCIENTIFIC CONTRIBUTION: This preliminary communication shows that SARS-CoV2 S protein features a potential estrogen binding site. Hopefully, this will prompt a more comprehensive study on the possibilities of estrogen binding on the S protein and the effect this might confer on the virus infectivity.
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spelling pubmed-81570852021-06-02 SARS-Cov2 S Protein Features Potential Estrogen Binding Site Tomasović, Ante Stanzer, Damir Krešimir Svetec, Ivan Svetec Miklenić, Marina Food Technol Biotechnol Preliminary Communications RESEARCH BACKGROUND: During the current SARS-CoV2 pandemic, as well as earlier SARS and MERS epidemics, it has been observed that COVID19-positive women on average tend to have milder symptoms and lower fatality rates than men. There is a number of differences between the sexes known to contribute to different immune responses and severity of the disease, one being the effect of estrogen via estrogen receptor signalling. We wondered if estrogen might also affect the SARS-CoV2 more directly, perhaps by binding to the surface glycoprotein (S protein), thus possibly reducing its infectivity. EXPERIMENTAL APPROACH: To assess whether there is a possibility for estrogen binding on the SARS-CoV2 S protein, we used BLAST and HHpred to compare protein sequences of S protein and human estrogen receptor β, while 3D structures of a potential estrogen binding site and an active site of estrogen receptor β were visualized and compared using PyMOL. RESULTS AND CONCLUSIONS: By comparing the sequence of SARS-CoV2 S protein with the human estrogen receptor β, we identified a potential estrogen binding site on S protein and further determined that it also shares notable similarities with the active site of ER β when observed in 3D structure of their respective proteins. As a control, SARS-CoV2 S protein was compared with the human androgen receptor, and no such similarities were found. The potential estrogen binding site is part of coronavirus S2 superfamily domain, which is involved in host-virus membrane fusion during infection and appears to be conserved throughout the Coronaviridae family. NOVELTY AND SCIENTIFIC CONTRIBUTION: This preliminary communication shows that SARS-CoV2 S protein features a potential estrogen binding site. Hopefully, this will prompt a more comprehensive study on the possibilities of estrogen binding on the S protein and the effect this might confer on the virus infectivity. University of Zagreb Faculty of Food Technology and Biotechnology 2021-03 /pmc/articles/PMC8157085/ /pubmed/34084077 http://dx.doi.org/10.17113/ftb.59.01.21.6820 Text en https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC BY) 4.0 License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Preliminary Communications
Tomasović, Ante
Stanzer, Damir
Krešimir Svetec, Ivan
Svetec Miklenić, Marina
SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title_full SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title_fullStr SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title_full_unstemmed SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title_short SARS-Cov2 S Protein Features Potential Estrogen Binding Site
title_sort sars-cov2 s protein features potential estrogen binding site
topic Preliminary Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157085/
https://www.ncbi.nlm.nih.gov/pubmed/34084077
http://dx.doi.org/10.17113/ftb.59.01.21.6820
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