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