02025nam a2200277Ia 4500 MX-MdCICY 20260521091709.0 CICY B-19679 Structure-function analysis reveals Trichoderma virens Tsp1 to be a novel fungal effector protein modulating plant defence International Journal of Biological Macromolecules, 191, p.267-276, 2021 Trichoderma virens colonizes roots and develops a symbiotic relationship with plants where the fungal partner derives nutrients from plants and offers defence, in return. Tsp1, a small secreted cysteine-rich protein, was earlier found to be upregulated in co-cultivation of T. virens with maize roots. Tsp1 is well conserved in Ascomycota division of fungi, but none of its homologs have been studied yet. We have expressed and purified recombinant Tsp1, and resolved its structure to 1.25 Å resolutions, from two crystal forms, using Se-SAD methods. The Tsp1 adopts a ? barrel fold and forms dimer in structure as well as in solution form. DALI based structure analysis revealed the structure similarity with two known fungal effector proteins: Alt a1 and PevD1. Structure and evolutionary analysis suggested that Tsp1 belongs to a novel effector protein family. Tsp1 acted as an inducer of salicylic acid mediated susceptibility in plants, rendering maize plants more susceptible to a necrotrophic pathogen Cochliobolus heterostrophus, as observed using plant defence assay and RT-qPCR analysis. BETA-BARREL FOLD PROTEIN EFFECTOR SYMBIOSIS TRICHODERMA TSP1 Gupta, G. D. Bansal, R. Mistry, H. Pandey, B. Mukherjee, P. K. https://drive.google.com/file/d/1IS3S3xLbdJi0hSIimPcQp4cg6CuEZ1-r/view?usp=drivesdk Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx Loc REF1 250602s9999 xx |||||s2 |||| ||und|d 29741 29741 0 0 Loc 0 0 F1 CICY CICY RE 2025-06-25 0 B-19679 2025-06-25 16:24:35 2025-06-25 REF1