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--- bacteria:t3e:xopq [2026/10/29 15:07] – [References] rkoebnik
+++ bacteria:t3e:xopq [2026/10/29 15:14] (current) – [Biological function] rkoebnik
@@ Line 37: / Line 37: @@
   * XopQ suppressed cell death reactions in //N. benthamiana//  that were triggered by three //Xcv//  type III effectors (XopB, XopJ, XopL), whereas cell death reactions triggered by AvrBsT were not suppressed by XopQ (Adlung, 2016).
   * XopQ-mediated cell death suppression in //N. benthamiana//  during transient expression assays was later shown to result from an attenuation of //Agrobacterium//  ‐mediated protein expression rather than reflecting a genuine XopQ virulence activity (Adlung & Bonas, 2017).
-  * A Δ//xopN//–Δ//xopQ// double knock-out mutant in //X. phaseoli//  pv. //manihotis//  (//Xpm//) was less aggressive in the cassava host plant than its single mutation counterparts. In addition, //in planta //  bacterial growth was reduced at 5 dpi in the double mutant with respect to the wild-type strain CIO151 and individual knock-out strains. The phenotype of the double mutant could be complemented when transforming a plasmid containing //xopQ//. These results confirmed that //xopN //and// xopQ //are functionally redundant in //Xpm//  (Medina //et al.//, 2017).
+  * A Δ//xopN//–Δ//xopQ//  double knock-out mutant in //X. phaseoli//  pv. //manihotis//  (//Xpm//) was less aggressive in the cassava host plant than its single mutation counterparts. In addition, //in planta //  bacterial growth was reduced at 5 dpi in the double mutant with respect to the wild-type strain CIO151 and individual knock-out strains. The phenotype of the double mutant could be complemented when transforming a plasmid containing //xopQ//. These results confirmed that //xopN //and// xopQ //are functionally redundant in //Xpm//  (Medina //et al.//, 2017).
   * A reverse genetics screen identified Recognition of XopQ 1 (Roq1), a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, which mediates XopQ recognition in //N. benthamiana//. Roq1 orthologs appear to be present only in the //Nicotiana//  genus. Expression of Roq1 was found to be sufficient for XopQ recognition in both the closely-related //Nicotiana sylvestris//  and the distantly-related beet plant (//Beta vulgaris//) (Schultink //et al.//, 2017).
   * Roq1 is able to recognize XopQ alleles from various //Xanthomonas//  species, as well as HopQ1 from //Pseudomonas//, demonstrating widespread potential application in protecting crop plants from these pathogens (Schultink //et al.//, 2017).
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   * A screen for //Xanthomonas//  effectors which can suppress XopQ-XopX induced rice immune responses, led to the identification of five effectors, namely XopU, XopV, XopP, XopG and AvrBs2, that could individually suppress these immune responses. These results suggest a complex interplay of //Xanthomonas//  T3SS effectors in suppression of both pathogen-triggered immunity and effector-triggered immunity to promote virulence on rice (Deb //et al.//, 2020).
   * Expression of XopQ in In //N. benthamiana//  triggers Roq1-dependent effector-triggered immunity (ETI) responses accompanied by the accumulation of plastids around the nucleus and the formation of stromules. It was shown that XopQ-triggered plastid clustering is not strictly linked to stromule formation during ETI and that stromule formation, in contrast to chloroplast perinuclear dynamics, is an integral part of the //N. benthamiana//  ETI response, where both NRG1 and ADR1 play a role in this ETI response (Prautsch //et al.//, 2023).
+  * Deletion of //xopQ<sub>Xcc</sub> //  increased disease indices by more than 10% in cabbage line G1180, while bacterial counts also increased (Chen //et al.//, 2026).
+  * Transient expression of XopQ<sub>//Xcc// </sub>  triggered a hypersensitive response in cabbage, and reverse transcription quantitative PCR (RT-qPCR) analyses revealed that XopQ suppressed the expression of a WRKY transcription factor gene (WRKY33) associated with pattern-triggered immunity (Chen //et al.//, 2026)
 === Localization ===
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 Using protein-protein interaction studies in yeast and in planta, XopQ<sub>Xcv</sub>  was shown to physically interacts with the 14–3–3 protein TFT4 from tomato (//Solanum lycopersicum//) (Teper //et al.//, 2014). A mutation in the putative 14–3–3 binding site of XopQ (S65A) impaired interaction of the effector with TFT4 from pepper and tomato (//Capsicum annuum//) and its virulence function //in planta//  (Teper //et al.//, 2014). Yeast 2-hybrid assays revealed that XopQ<sub>Xcv</sub>  interacts with multiple, but perhaps not all 14–3–3 protein isoforms (Teper //et al.//, 2014; Dubrov //et al.//, 2018).
-Bimolecular fluorescence complementation assays upon transient expression in //N. benthamiana//  using split-YFP derivatives revealed that XopQ may interact with itself and also with XopS, maybe forming a large protein complex //in planta// (Adlung, 2016).
+Bimolecular fluorescence complementation assays upon transient expression in //N. benthamiana//  using split-YFP derivatives revealed that XopQ may interact with itself and also with XopS, maybe forming a large protein complex //in planta//  (Adlung, 2016).
 Roq1 (__R__ecognition of X__o__p__Q__), a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, was found to co-immunoprecipitate with XopQ, for the first time suggesting a physical association between the two proteins (Schultink //et al.//, 2017). Structural biology later demonstrated that ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome complex that brings together the TIR domains for downstream immune signaling (Martin //et al.//, 2020).

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