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...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-07-01
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| Series: | Biochemistry and Biophysics Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580821000765 |
| _version_ | 1818837264043606016 |
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| author | Tamim Ahsan Abu Ashfaqur Sajib |
| author_facet | Tamim Ahsan Abu Ashfaqur Sajib |
| author_sort | Tamim Ahsan |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-19T03:19:44Z |
| format | Article |
| id | doaj.art-81fa37ca2027411389aeec19c5705fd4 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-19T03:19:44Z |
| publishDate | 2021-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-81fa37ca2027411389aeec19c5705fd42022-12-21T20:37:49ZengElsevierBiochemistry and Biophysics Reports2405-58082021-07-0126100982Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptorTamim Ahsan0Abu Ashfaqur Sajib1Department of Genetic Engineering & Biotechnology, Bangabandhu Sheikh Mujibur Rahman Maritime University, Dhaka, 1216, BangladeshDepartment of Genetic Engineering & Biotechnology, University of Dhaka, Dhaka, 1000, Bangladesh; Corresponding author.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.http://www.sciencedirect.com/science/article/pii/S2405580821000765COVID-19SARS-CoV-2Spike proteinACE1ACE2Host-virus interaction |
| spellingShingle | Tamim Ahsan Abu Ashfaqur Sajib Repurposing of approved drugs with potential to interact with SARS-CoV-2 receptor Biochemistry and Biophysics Reports COVID-19 SARS-CoV-2 Spike protein ACE1 ACE2 Host-virus interaction |
| 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 | COVID-19 SARS-CoV-2 Spike protein ACE1 ACE2 Host-virus interaction |
| url | http://www.sciencedirect.com/science/article/pii/S2405580821000765 |
| work_keys_str_mv | AT tamimahsan repurposingofapproveddrugswithpotentialtointeractwithsarscov2receptor AT abuashfaqursajib repurposingofapproveddrugswithpotentialtointeractwithsarscov2receptor |