Aim And Objectives:
Phytophthora infestans (Mont.) de Bary, fungal pathogen it causes late blight, which results
in devastating economic loss among the Solanaceae. The bacillus lipopeptides shows the antagonistic activity against the
many plant pathogens, among bacillus lipopeptides Iturin A reported as the antifungal gene. Hence, to understand the in silico antifungal activity, we have selected gene iturin A (AXN89987) produced by Bacillus spp to check the molecular dynamics study with the effector proteins of the P. infestanse. In this concern known effectors proteins of P. infestans were subjected to the protein-protein interaction and followed by simulation.
Material and Method:
Iturin A gene was amplified using the soil bacterium Bacillus subtilis with gene specific primers.
Cloned into pTZ 57R/T vector and confirmed by sequencing. To get better insight the protein model was developed for Iturin A using Modeller 9.17, also for the effector proteins by using PDB structure of ID 4MRT (Phosphopantetheine Transferase Sfp) and 1QR0 (4'-phosphopantetheinyl moiety of coenzyme A) as template it shares the identity 72% and expected
P-value: 3e-121 respectively. The model quality was assessed using ProSA and PROCHECK programs.
Results:
The potency of modelled protein against effector proteins of P. infestans were evaluated in silico using the
HADDOCK server and the results showed the high affinity of Iturin A toward the effector protein Host ATG8 (PDB-5L83).
Finally, the simulation was performed to the docked conformation of Iturin A with Host ATG8 to further understand the
stability of the complex using Desmond program.
Conclusion:
Altogether the protein-protein interaction and simulation study propose a new methodology and intern it also
attempted to uncover possible antifungal activity of iturin A against effector proteins of P. infestans.
Investigation of the Josephin Domain Protein-Protein Interaction by Molecular Dynamics
