In Silico ANALYSIS OF PROTEIN - PROTEIN INTERACTION BETWEEN RESISTANCE AND VIRULENCE PROTEIN DURING LEAF RUST DISEASE IN WHEAT (Triticum aestivum L.)

KUMAR A.¹, MISHRA D.C.², RAI A.³, SHARMA M.K.⁴, GAJULA M.N.V.P.^5
1Centre for Agricultural Bioinformatics, IASRI, Library Avenue, New Delhi-110012, India.
²Centre for Agricultural Bioinformatics, IASRI, Library Avenue, New Delhi-110012, India.
³Centre for Agricultural Bioinformatics, IASRI, Library Avenue, New Delhi-110012, India.
⁴Department of Bioinformatics, J.V. College, Baraut-250 611, UP, India.
⁵Centre for Agricultural Bioinformatics, IASRI, Library Avenue, New Delhi-110012, India.

Received : 14-11-2013     Accepted : 05-12-2013     Published : 28-12-2013
Volume : 2     Issue : 1       Pages : 52 - 58
World Res J Pept Protein 2.1 (2013):52-58

Wheat is a staple cereal crop and major food resource for majority population all over the world and it suffers from leaf rust disease which causes substantial loss in yield as well as grain quality. The leaf rust is a fungus disease caused by fungus P. recondita f.sp. tritici. Lr1, Lr10, Lr19, Lr34, Lr47 and Lr51 are resistance genes among many others while MAPK1 is a fungus protein causing leaf rust in wheat. Chemical control of rusts is expensive and hazardous to the environment. In present In silico study we generated the structure of MAPK1 and leaf rust resistance protein Lr1, Lr10, Lr19, Lr34, Lr47 and Lr51 using homology modeling. Reliability of the homology model was assessed by predicting MAPK1 secondary structure along with validation. The MAPK1 3D model was further evaluated by energy minimization algorithm. Protein-protein interaction between MAPK1 and leaf rust resistance proteins was studied by using a geometrical based docking program Patch Dock. Based on the result of protein-protein docking score and total atomic contact energy (ACE), interaction of MAPK1 was reported to be high with Lr51 and lowermost with Lr10. Furthermore force field studies also supported this phenomenon. The minimum docking score of Lr10 to MAPK1 indicate that it does not directly interact with pathogen protein during rust infection. It could be suggested that Lr51 is more interactive with MAPK1 then other leaf rust resistance genes which are found in wheat against rust disease. The results presented here could be useful in designing alternative resistance genes against wheat leaf rust disease.

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