Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 191, Issue -, Pages 267-276Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.09.085
Keywords
Beta-barrel fold protein; Effector; Symbiosis; Trichoderma; Tsp1
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Trichoderma virens colonizes roots and forms a symbiotic relationship with plants, deriving nutrients from plants and offering defense in return. Tsp1, a cysteine-rich protein, acts as an inducer of susceptibility in plants. Evolutionary analysis suggests Tsp1 belongs to a novel effector protein family.
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 angstrom resolutions, from two crystal forms, using Se-SAD methods. The Tsp1 adopts a beta 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.
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