TIR-Lectin two-domain protein confers defence properties against spider mite attack

One protein with two domains, lectin and Toll-IL receptor is able to alter not only JA and SA but also different hormonal levels and to confer defence properties in plants against the phytophagous acari Tetranychus urticae.


Plant immunity depends on fast and specific transcriptional reprogramming triggered by the perception of biotic stresses. Numerous studies have been conducted to better understand the response of plants to the generalist herbivore two-spotted spider mite (Tetranychus urticae). However, how plants perceive mites and how this perception is translated into changes in gene expression are largely unknown. In this work, we identified a gene induced in Arabidopsis (Arabidopsis thaliana) upon spider mite attack that encodes a two-domain protein containing predicted lectin and Toll-IL receptor domains. The gene, previously named PP2-A5, belongs to the Phloem Protein2 family. Biotic assays showed that PP2-A5 confers tolerance to T. urticae. Overexpression or knockout of PP2-A5 leads to transcriptional reprogramming that alters the balance of hormone accumulation and corresponding signalling pathways. The nucleocytoplasmic location of this protein supports a direct interaction with regulators of gene transcription, suggesting that the combination of two putative signalling domains in a single protein may provide a novel mechanism for regulating gene expression. Together, our results show that PP2-A5 improves the ability to defend against T. urticae by participating in the tight regulation of hormonal cross talk upon mite feeding. Further research is needed to determine the mechanism by which this two-domain protein functions and to clarify its molecular role in signalling following a spider mite attack.


Original Paper:

Santamaria, M.E., Martinez, M., Arnaiz, A., Rioja, C., Burow, M., Grbic, V., Diaz, I. 2019. An Arabidopsis TIR-lectin two-domain protein confers defence properties against Tetranychus urticae. Plant Physiology pp.00951.2018. DOI: 10.1104/pp.18.00951