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bacteria:t3e:xopc [2023/05/17 12:28] – [XopC] rkoebnikbacteria:t3e:xopc [2026/06/22 12:09] (current) – [Biological function] rkoebnik
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-====== XopC ======+====== The Type III Effector XopC from //Xanthomonas// ======
  
 Author: [[https://www.researchgate.net/profile/Alice_Castaing|Alice Boulanger]]\\ Author: [[https://www.researchgate.net/profile/Alice_Castaing|Alice Boulanger]]\\
 Internal reviewer: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]]\\ Internal reviewer: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]]\\
-Expert reviewer: FIXME 
  
 Class: XopC\\ Class: XopC\\
-Family: XopC\\+Families: XopC1 and XopC2\\
 Prototype (XopC1): XCV2435 (//Xanthomonas euvesicatoria// pv. //euvesicatoria//, ex //Xanthomonas campestris// pv. //vesicatoria//; strain 85-10)\\ Prototype (XopC1): XCV2435 (//Xanthomonas euvesicatoria// pv. //euvesicatoria//, ex //Xanthomonas campestris// pv. //vesicatoria//; strain 85-10)\\
 GenBank ID (XopC1): [[https://www.ncbi.nlm.nih.gov/protein/CAJ24112.1|CAJ24112.1]] (834 aa)\\ GenBank ID (XopC1): [[https://www.ncbi.nlm.nih.gov/protein/CAJ24112.1|CAJ24112.1]] (834 aa)\\
-Prototype (XopC2): XOC_1264 (//Xanthomonas oryzae// pv. // oryzicola //; strain BLS256)\\+Prototype (XopC2): XOC_1264 (//Xanthomonas oryzae// pv. //oryzicola//; strain BLS256)\\
 GenBank ID (XopC2): [[https://www.ncbi.nlm.nih.gov/protein/AEQ95452.1|AEQ95452.1]] (549 aa - likely too short)\\ GenBank ID (XopC2): [[https://www.ncbi.nlm.nih.gov/protein/AEQ95452.1|AEQ95452.1]] (549 aa - likely too short)\\
 GenBank ID (XopC2; strain GX01): [[https://www.ncbi.nlm.nih.gov/protein/QEO98660.1|QEO98660.1]] (596 aa)\\ GenBank ID (XopC2; strain GX01): [[https://www.ncbi.nlm.nih.gov/protein/QEO98660.1|QEO98660.1]] (596 aa)\\
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 === How discovered? === === How discovered? ===
  
-XopC was discovered in //X. campestris// pv. //vesicatoria// (//Xcv//) in a cDNA-AFLP screen (Noël //et al//., 2001). XopC was also identified in a genetic screen, using a Tn//5//-based transposon construct harboring the coding sequence for the HR-inducing domain of AvrBs2, but devoid of the effectors' T3SS signal, that was randomly inserted into the genome of //Xcv //strain 85-10. The XopC::AvrBs2 fusion protein triggered a //Bs2//-dependent hypersensitive response (HR) in pepper leaves (Roden //et al//., 2004).+XopC was discovered in //X. campestris// pv. //vesicatoria// (//Xcv//) in a cDNA-AFLP screen (Noël //et al//., 2001). XopC was also identified in a genetic screen, using a Tn//5//-based transposon construct harboring the coding sequence for the HR-inducing domain of AvrBs2, but devoid of the effectors' T3SS signal, that was randomly inserted into the genome of //Xcv//strain 85-10. The XopC::AvrBs2 fusion protein triggered a //Bs2//-dependent hypersensitive response (HR) in pepper leaves (Roden //et al//., 2004).
 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
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   * The absence of //xopC//  in the genome of //Xcv//  led to an accelerated AvrBs1-induced HR in resistant pepper plants, if the plants were additionally stressed by exogenous application of salicylic acid (SA). This phenotype was complemented by //xopC//, but not by a //xopC//  derivative carrying a mutation in the predicted HAD-like hydrolase sequence (Herzfeld, 2013).   * The absence of //xopC//  in the genome of //Xcv//  led to an accelerated AvrBs1-induced HR in resistant pepper plants, if the plants were additionally stressed by exogenous application of salicylic acid (SA). This phenotype was complemented by //xopC//, but not by a //xopC//  derivative carrying a mutation in the predicted HAD-like hydrolase sequence (Herzfeld, 2013).
   * Virus-induced gene silencing (VIGS) of OAS-TL in planta abolished the acceleration of AvrBs1-mediated HR formation induced by the absence of //xopC//  in //Xcv//  in resistant pepper plants dependent on SA. These data suggest, that the induction of the AvrBs1-dependent HR in resistant pepper plants is SA-stress dependently delayed by XopC, which is reliant on a HAD-like hydrolase domain in XopC. This delay is mediated by the XopC plant interaction partner OAS-TL. Furthermore, expression analysis showed an increased accumulation of β-1,3-Glucanase transcript in //Xcv//-infected, resistant pepper plants by the presence of //xopC//. These findings indicated that XopC influences different mechnisms of the plant metabolism (Herzfeld, 2013).   * Virus-induced gene silencing (VIGS) of OAS-TL in planta abolished the acceleration of AvrBs1-mediated HR formation induced by the absence of //xopC//  in //Xcv//  in resistant pepper plants dependent on SA. These data suggest, that the induction of the AvrBs1-dependent HR in resistant pepper plants is SA-stress dependently delayed by XopC, which is reliant on a HAD-like hydrolase domain in XopC. This delay is mediated by the XopC plant interaction partner OAS-TL. Furthermore, expression analysis showed an increased accumulation of β-1,3-Glucanase transcript in //Xcv//-infected, resistant pepper plants by the presence of //xopC//. These findings indicated that XopC influences different mechnisms of the plant metabolism (Herzfeld, 2013).
-  * XopC2 of //X. citri //pv. //punicae//  was found to contribute to the bacterial blight development on pomegranate fruit plants. Xap //ΔxopC2//  was demonstrated to cause reduced the blight lesions when inflitrated on pomegranate leaves, induce defense responses like callose deposition, ROS production and upregulate immune-responsive genes in its natural host plants (Mondal //et al.//, 2020). +  * XopC2 of //X. citri//  pv. //punicae//  was found to contribute to the bacterial blight development on pomegranate fruit plants. Xap //ΔxopC2//  was demonstrated to cause reduced the blight lesions when inflitrated on pomegranate leaves, induce defense responses like callose deposition, ROS production and upregulate immune-responsive genes in its natural host plants (Mondal //et al.//, 2020). 
-  * Ectopic expression of XopC2 was found to promote jasmonate signaling and stomatal opening in transgenic rice plants, which were more susceptible to //X. oryzae// pv. //oryzicola// infection (Wang //et al.//, 2021).+  * Ectopic expression of XopC2 was found to promote jasmonate signaling and stomatal opening in transgenic rice plants, which were more susceptible to //X. oryzae//  pv. //oryzicola//  infection (Wang //et al.//, 2021). 
 +  * The small regulatory noncoding RNA (sRNA) Xonc3711 was found to repress production of the DNA-binding protein Xoc_3982 by binding to the xoc_3982 mRNA, and both ChIP-seq and electrophoretic mobility shift assays showed that Xoc_3982 repressed the transcription of the effector XopC2, which contributes to virulence in //Xoc// <sub>BLS256</sub>  (Wu //et al.//, 2021). 
 +  * XopC2 from //Xanthomonas phaseoli//  pv. //manihotis//  was found to repress host immune responses in cassava, thus promoting bacterial pathogen infection (Wei //et al.//, 2024).
  
 === Localization === === Localization ===
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 === Interaction partners === === Interaction partners ===
  
-Yeast-2-hybrid studies revealed a XopC interactor, which also interacted with XopC in planta. The interactor localises to the plant cell cytoplasm and carries typical features of plant cytosolic O-acetylserine (thiol)lyases (OAS-TL). It shows OAS-TL activity in vivo and in vitro. The latter one is enhanced by adding XopC (Herzfeld, 2013).+Yeast-2-hybrid studies revealed a XopC interactor, which also interacted with XopC //in planta//. The interactor localises to the plant cell cytoplasm and carries typical features of plant cytosolic //O//-acetylserine (thiol)lyases (OAS-TL). It shows OAS-TL activity //in vivo//  and //in vitro//. The latter one is enhanced by adding XopC (Herzfeld, 2013). 
 + 
 +XopC2 from //Xanthomonas phaseoli//  pv. //manihotis//  physically associated with MeHSP90.9 from cassava to inhibit its interaction with MeCPK1 and the corresponding protein phosphorylation by MeCPK1, so as to repress host immune responses and promote bacterial pathogen infection (Wei //et al.//, 2024).
  
 ===== Conservation ===== ===== Conservation =====
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 The distantly related XopC2 has homologs in //X. citri//, //X. axonopodis//, //X. euvesicatoria//, //X. oryzae//, //X. phaseoli//, and //X. translucens// (BLASTP and TBLASTN performed in June 2020) The distantly related XopC2 has homologs in //X. citri//, //X. axonopodis//, //X. euvesicatoria//, //X. oryzae//, //X. phaseoli//, and //X. translucens// (BLASTP and TBLASTN performed in June 2020)
-=== In other plant pathogens/symbionts === 
  
-XopC1: //Ralstonia solanacearum// (RipC2), //Trinickia caryophylli// (//Paraburkholderia caryophylli//), //Xylophilus ampelinus// (BLASTP and TBLASTN performed in June 2020). 
- 
-XopC2: //Acidovorax// ssp., //Pseudomonas cissicola//, //Ralstonia solanacearum// (RipC1) (BLASTP and TBLASTN performed in June 2020). 
- 
-===== Conservation ===== 
- 
-=== In xanthomonads === 
- 
-Close, full-length homologs (>90% sequence identity) of XopC1 have only been found in several strains of clade-2 xanthomonads, such as //X. citri//, //X. euvesicatoria//, //X. fragariae//, //X. gardneri//, //X. hortorum//, and //X. phaseoli// (BLASTP and TBLASTN performed in June 2020). 
- 
-The distantly related XopC2 has homologs in //X. citri//, //X. axonopodis//, //X. euvesicatoria//, //X. oryzae//, //X. phaseoli//, and //X. translucens// (BLASTP and TBLASTN performed in June 2020) 
 === In other plant pathogens/symbionts === === In other plant pathogens/symbionts ===
  
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 Szurek B, Rossier O, Hause G, Bonas U (2002). Type III-dependent translocation of the //Xanthomonas// AvrBs3 protein into the plant cell. Mol. Microbiol. 46: 13-23. DOI: [[https://doi.org/10.1046/j.1365-2958.2002.03139.x|10.1046/j.1365-2958.2002.03139.x]] Szurek B, Rossier O, Hause G, Bonas U (2002). Type III-dependent translocation of the //Xanthomonas// AvrBs3 protein into the plant cell. Mol. Microbiol. 46: 13-23. DOI: [[https://doi.org/10.1046/j.1365-2958.2002.03139.x|10.1046/j.1365-2958.2002.03139.x]]
  
-Wang S, Li S, Wang J, Li Q, Xin XF, Zhou S, Wang Y, Li D, Xu J, Luo ZQ, He SY, Sun W (2021). A bacterial kinase phosphorylates OSK1 to suppress stomatal immunity in rice. Nat. Commun.12: 5479. doi: [[https://doi.org/10.1038/s41467-021-25748-4|10.1038/s41467-021-25748-4]]+Wang S, Li S, Wang J, Li Q, Xin XF, Zhou S, Wang Y, Li D, Xu J, Luo ZQ, He SY, Sun W (2021). A bacterial kinase phosphorylates OSK1 to suppress stomatal immunity in rice. Nat. Commun.12: 5479. DOI: [[https://doi.org/10.1038/s41467-021-25748-4|10.1038/s41467-021-25748-4]] 
 + 
 +Wei Y, Zhu B, Zhang Y, Ma G, Wu J, Tang L, Shi H (2024). CPK1-HSP90 phosphorylation and effector XopC2-HSP90 interaction underpin the antagonism during cassava defense-pathogen infection. New Phytol. 242: 2734-2745. DOI: [[https://doi.org/10.1111/nph.19739|10.1111/nph.19739]] 
 + 
 +Wu Y, Wang S, Nie W, Wang P, Fu L, Ahmad I, Zhu B, Chen G (2021). A key antisense sRNA modulates the oxidative stress response and virulence in //Xanthomonas oryzae// pv. //oryzicola//. PLoS Pathog. 17: e1009762. DOI: [[https://doi.org/10.1371/journal.ppat.1009762|10.1371/journal.ppat.1009762]] 
 + 
 +===== Acknowledgements ===== 
 + 
 +This fact sheet is based upon work from COST Action CA16107 EuroXanth, supported by COST (European Cooperation in Science and Technology).
  
bacteria/t3e/xopc.1684322893.txt.gz · Last modified: 2023/05/17 12:28 by rkoebnik

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