s Efficiency of CAT and L-SIGN as Alternative or Co-receptors for SARSCoV- 2 Spike Protein

Background: The COVID-19 disease, which is caused by SARS-CoV-2, has been spreading rapidly over the world since December 2019 and has become a serious threat to human health. According to reports, SARS-CoV-2 infection has an impact on several human tissues, including the kidney, gastrointestinal system, and lungs. The Spike (S) protein from SARS-CoV-2 has been found to primarily bind ACE2. Since the lungs are the organ that COVID-19 is most likely to infect, the comparatively low expression of this recognized receptor suggests that there may be alternative coreceptors or alternative SARS-CoV-2 receptors that cooperate with ACE2. Recently, many candidate receptors of SARS-CoV-2 other than ACE2 were reported to be specifically and highly expressed in SARS-CoV-2 affected tissues. Among these receptors, the binding affinity of CAT and L-SIGN to the S protein has been reported to be higher in one of the recent studies. So, it will be significant to understand the binding interactions between these potential receptors and the RBD region of the S protein.Objective: To perform a computational analysis to check the efficiency of the alternative receptors (CAT and L-SIGN) of the SARS-CoV-2 on its binding to the Receptor Binding Domain (RBD) of Spike protein (S protein).Methods: In this study, we compared the interaction profile of the RBD of the S protein of SARSCoV- 2 with CAT and L-SIGN receptors.Results: From the molecular dynamics simulation study, the S protein employs special techniques to have stable interactions with the CAT and L-SIGN receptors (ΔGbind = -39.49 kcal/mol and -37.20 kcal/mol, respectively).Conclusion: SARS-CoV-2 may result in greater virulence as a result of the S protein-CAT complex's stability and the greater affinity of spike protein for the CAT receptor.