Figure 1 : superimposition of the inhibitor bound EBOV VP35 complex (PDB code: 4BIC) with MARV VP35 (chain A of PDB code: 4GHA). The bound inhibitor is shown in ball and sticks, whereas the binding pocket is demarcated by a grid box highlighted in green. Also shown is a sequence alignment of EBOV VP35 with MARV VP35 with green highlights of conserved interacting residues of both proteins.
Results obtained from molecular docking simulations as presented inTable 3 provided insights into the possible binding mechanisms of the identified potential MARV VP35 inhibitors based on the interactions elicited upon binding. The highest negative docking score corresponded with the isolated that exhibited the highest potential binding to MARV VP35. Therefore, as shown in Table 3 , 1,2-Benzenedicarboxylic acid, butyl 2-methylpropyl ester (1,2BAB-2-MPE) with the highest binding affinity of -3.8kcal/mol exhibited the highest binding potential towards MARV VP35 amongst the identified anti-viral phytochemical compounds, whereas D-Limonene showed the least negative binding affinity of -3.1kcal/mol. . As a control, we also performed molecular docking of the known anti-filoviral drug FGI-103 (Warren et al., 2010) in the same active pocket. FGI-103 exhibited a relatively higher negative docking score of -4.1kcal/mol suggesting higher binding affinity than all the identified anti-viral phytochemicals.
Table 3: Tabular representation of docking scores of identified anti-viral phytochemical compounds of Spondias mombin against MARV VP35