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Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor
Respiratory transmission is the primary route of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) infection. Angiotensin I converting enzyme 2 (ACE2) is the known receptor of SARS-CoV-2 surface spike glycoprotein for entry into human cells. A recent study reported absent to low expressio...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8006196/ https://www.ncbi.nlm.nih.gov/pubmed/33817352 http://dx.doi.org/10.1016/j.bbrep.2021.100982 |
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author | Ahsan, Tamim Sajib, Abu Ashfaqur |
author_facet | Ahsan, Tamim Sajib, Abu Ashfaqur |
author_sort | Ahsan, Tamim |
collection | PubMed |
description | Respiratory transmission is the primary route of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) infection. Angiotensin I converting enzyme 2 (ACE2) is the known receptor of SARS-CoV-2 surface spike glycoprotein for entry into human cells. A recent study reported absent to low expression of ACE2 in a variety of human lung epithelial cell samples. Three bioprojects (PRJEB4337, PRJNA270632 and PRJNA280600) invariably found abundant expression of ACE1 (a homolog of ACE2 and also known as ACE) in human lungs compared to very low expression of ACE2. In fact, ACE1 has a wider and more abundant tissue distribution compared to ACE2. Although it is not obvious from the primary sequence alignment of ACE1 and ACE2, comparison of X-ray crystallographic structures show striking similarities in the regions of the peptidase domains (PD) of these proteins, which is known (for ACE2) to interact with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Critical amino acids in ACE2 that mediate interaction with the viral spike protein are present and organized in the same order in the PD of ACE1. In silico analysis predicts comparable interaction of SARS-CoV-2 spike protein with ACE1 and ACE2. In addition, this study predicts from a list of 1263 already approved drugs that may interact with ACE2 and/or ACE1 and potentially interfere with the entry of SARS-CoV-2 inside the host cells. |
format | Online Article Text |
id | pubmed-8006196 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-80061962021-03-29 Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor Ahsan, Tamim Sajib, Abu Ashfaqur Biochem Biophys Rep Research Article Respiratory transmission is the primary route of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) infection. Angiotensin I converting enzyme 2 (ACE2) is the known receptor of SARS-CoV-2 surface spike glycoprotein for entry into human cells. A recent study reported absent to low expression of ACE2 in a variety of human lung epithelial cell samples. Three bioprojects (PRJEB4337, PRJNA270632 and PRJNA280600) invariably found abundant expression of ACE1 (a homolog of ACE2 and also known as ACE) in human lungs compared to very low expression of ACE2. In fact, ACE1 has a wider and more abundant tissue distribution compared to ACE2. Although it is not obvious from the primary sequence alignment of ACE1 and ACE2, comparison of X-ray crystallographic structures show striking similarities in the regions of the peptidase domains (PD) of these proteins, which is known (for ACE2) to interact with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Critical amino acids in ACE2 that mediate interaction with the viral spike protein are present and organized in the same order in the PD of ACE1. In silico analysis predicts comparable interaction of SARS-CoV-2 spike protein with ACE1 and ACE2. In addition, this study predicts from a list of 1263 already approved drugs that may interact with ACE2 and/or ACE1 and potentially interfere with the entry of SARS-CoV-2 inside the host cells. Elsevier 2021-03-29 /pmc/articles/PMC8006196/ /pubmed/33817352 http://dx.doi.org/10.1016/j.bbrep.2021.100982 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Article Ahsan, Tamim Sajib, Abu Ashfaqur Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title | Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title_full | Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title_fullStr | Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title_full_unstemmed | Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title_short | Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor |
title_sort | repurposing of approved drugs with potential to interact with sars-cov-2 receptor |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8006196/ https://www.ncbi.nlm.nih.gov/pubmed/33817352 http://dx.doi.org/10.1016/j.bbrep.2021.100982 |
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