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Puccinia triticina effector protein Pt_21 interacts with wheat thaumatin-like protein TaTLP1 to inhibit its antifungal activity and suppress wheat apoplast immunity 被引量:4

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摘要 Puccinia triticina(Pt), as the causal agent of wheat leaf rust, employs a plethora of effector proteins to modulate wheat immunity for successful colonization. Understanding the molecular mechanisms underlying Pt effector-mediated wheat susceptibility remains largely unexplored. In this study, an effector Pt_21 was identified to interact with the apoplast-localized wheat thaumatin-like protein TaTLP1 using a yeast two-hybrid assay and the Pt_21-TaTLP1 interaction was characterized. The interaction between Pt_21 and TaTLP1 was validated by in vivo co-immunoprecipitation assay. A TaTLP1 variant,TaTLP1C71A, that was identified by the site-directed mutagenesis failed to interact with Pt_21. Pt_21was able to suppress Bax-mediated cell death in leaves of Nicotiana benthamiana and inhibit TaTLP1-mediated antifungal activity. Furthermore, infiltration of recombinant protein Pt_21 into leaves of transgenic wheat line overexpressing TaTLP1 enhanced the disease development of leaf rust compared to that in wild-type leaves. These findings demonstrate that Pt_21 suppresses host defense response by directly targeting wheat TaTLP1 and inhibiting its antifungal activity, which broadens our understanding of the molecular mechanisms underlying Pt effector-mediated susceptibility in wheat.
出处 《The Crop Journal》 SCIE CSCD 2023年第5期1431-1440,共10页 作物学报(英文版)
基金 supported by the National Natural Science Foundation of China (32172384 and 31501623) the Natural Science Foundation of Hebei (C2020204028) the Key Research and Development Project of Hebei Province (20326505D) the “Hundred Talents Program” for the Introduction of High-level Overseas Talents in Hebei Province (E2020100004)。
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