2.3. (a) Docking studies revealed preferential binding of Rv2615c protein with TLR4 than TLR2
TLRs in particular are essential for the recognition of the pathogenic Mtb proteins. The interaction of PE_PGRS proteins with TLRs has been shown in a number of studies (Abdallah et al. , 2007; Bansalet al. , 2010; Ramakrishnan, 2012; Grover et al. , 2018; Liuet al. , 2020). I-TASSER homology modelled Rv2615c protein docking experiments with TLR2 and TLR4 demonstrated Rv2615c’s strong affinity for TLR4 binding (Fig 3a). HADDOCK predicted a score of -141.3±13.8 for Rv2615c-TLR4 docked complex while -109.5±5.8 for Rv2615c-TLR2 docked complex. The TLR2-Rv2615c complex had a total of 46 structures, which were grouped into 9 clusters, whereas the TLR4-Rv2615c complex had 67 structures, which were grouped into 9 clusters. TLR2 and Rv2615c complexes were predicted to have the best Z scores, with -2 for TLR2 and -1.7 for Rv2615c.