Version 1
: Received: 19 April 2020 / Approved: 20 April 2020 / Online: 20 April 2020 (16:01:29 CEST)
Version 2
: Received: 30 July 2020 / Approved: 2 August 2020 / Online: 2 August 2020 (09:23:18 CEST)
How to cite:
Sajib, A. Repurposing of Approved Drugs with Potential to Interact with SARS-CoV-2 Receptor. Preprints2020, 2020040369. https://doi.org/10.20944/preprints202004.0369.v2
Sajib, A. Repurposing of Approved Drugs with Potential to Interact with SARS-CoV-2 Receptor. Preprints 2020, 2020040369. https://doi.org/10.20944/preprints202004.0369.v2
Sajib, A. Repurposing of Approved Drugs with Potential to Interact with SARS-CoV-2 Receptor. Preprints2020, 2020040369. https://doi.org/10.20944/preprints202004.0369.v2
APA Style
Sajib, A. (2020). Repurposing of Approved Drugs with Potential to Interact with SARS-CoV-2 Receptor. Preprints. https://doi.org/10.20944/preprints202004.0369.v2
Chicago/Turabian Style
Sajib, A. 2020 "Repurposing of Approved Drugs with Potential to Interact with SARS-CoV-2 Receptor" Preprints. https://doi.org/10.20944/preprints202004.0369.v2
Abstract
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, potentially interfere with the entry of SARS-CoV-2 inside the host cells and alleviate the symptoms of Coronavirus disease (COVID-19).
Keywords
COVID-19; SARS-CoV-2; spike protein; ACE1; ACE2; host-virus interaction; drug repurposing
Subject
Biology and Life Sciences, Virology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Commenter: Abu Sajib
Commenter's Conflict of Interests: Author