In silico Analysis of Interaction between SARS-CoV-2 Membrane Protein and Human AKR1C2 Protein Revealed Universally Conserved Binding Site

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for an ongoing COVID-19 pandemic that has devastated mankind. During this pandemic, it has been observed that the mortality rate in men is markedly higher than that in women. The SARS-CoV-2 membrane protein plays a decisive role in the viral life cycle. In infected people, membrane protein impedes the conversion of testosterone from active form to its inactive form via its interaction with human Aldo-keto reductase family 1 member C2 protein. This leads to the high availability of active testosterone which in turn promotes the SARS-CoV-2 entry into the host cell. In the present study, in silico analysis of interaction between membrane protein and Aldo-keto reductase family 1 member C2 protein and conservation analysis of 16,39,480 SARS-CoV-2 membrane protein revealed novel universally conserved binding  site. Targeting this conserved binding site with small drug-like molecules would inhibit the interaction which leads to inhibition of SARS-CoV-2 entry into the host cell.