Proteomic analysis reveals different sets of proteins expressed during high temperature stress in two thermotolerant isolates of Trichoderma
Several species of the soil borne fungus of the genus Trichoderma are known to be versatile, opportunistic plant symbionts, and are the most successful biocontrol agents used in todays agriculture. To be successful in the field conditions, the fungus must endure varying climatic conditions. Studies have indicated that high atmospheric temperature coupled with low humidity is a major limitation for the inconsistent performance of Trichoderma under field conditions. Understanding the molecular modulation associated with such Trichoderma that persist and deliver under abiotic stress condition will aid in exploiting the worth of these organisms for such use. In this study, comparative proteomic analysis using two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption/time-of-flight (MALDI-TOF-TOF) mass spectrometry was used to identify proteins associated with thermotolerance in two thermotolerant isolates of Trichoderma--T. longibrachiatum 673, TaDOR673 and T. asperellum 7316, TaDOR7316--and 32 differentially expressed proteins were identified. Sequence homology and conserved domains were used to identify these proteins and to assign probable function to them. Thermotolerant isolate, TaDOR673, seemed to employ the stress signaling MAPK pathways and heat shock response pathways to combat the stress condition whereas the moderately tolerant isolate, TaDOR7316, seemed to adapt to high temperature conditions by reducing the accumulation of mis-folded proteins through unfolded protein response pathway and autophagy. Also, there were unique as well as common proteins that were differentially expressed in the two isolates studied.