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bacteria:t3e:xopd [2020/07/08 17:27] – [Biological function] rkoebnikbacteria:t3e:xopd [2025/02/12 23:51] (current) – jfpothier
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-====== XopD ======+====== The Type III Effector XopD from //Xanthomonas// ======
  
 Author: [[https://www.researchgate.net/profile/Monika_Kaluzna|Monika Kałużna]]\\ Author: [[https://www.researchgate.net/profile/Monika_Kaluzna|Monika Kałużna]]\\
-Internal reviewer: [[https://www.researchgate.net/profile/Alice_Castaing|Alice Boulanger]]\\ +Internal reviewer: [[https://www.researchgate.net/profile/Alice_Castaing|Alice Boulanger]]
-Expert reviewer: FIXME+
  
-Class: XopD (Xanthomonas outer protein D)\\+Class: XopD (//Xanthomonas// outer protein D)\\
 Family: XopD\\ Family: XopD\\
-Prototype: XopD (//Xanthomonas euvesicatoria// pv. //euvesicatoria//, ex //Xanthomonas campestris// pv. //vesicatoria//; strain 85-10)\\ +Prototype: XCV0437 (//Xanthomonas euvesicatoria// pv. //euvesicatoria//, ex //Xanthomonas campestris// pv. //vesicatoria//; strain 85-10)\\ 
-RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/CAJ22068|CAJ22068]] (545 aa); [[https://www.ncbi.nlm.nih.gov/protein/DAA34040|DAA34040]] (760 aa) new annotation\\ +GenBank ID: [[https://www.ncbi.nlm.nih.gov/protein/CAJ22068.1|CAJ22068.1]] (545 aa; original but wrong structural annotation)\\ 
-3D structure: [[https://www.rcsb.org/structure/2OIV|2OIV]], [[https://www.rcsb.org/structure/2OIX|2OIX]] (Chosed //et al//., 2007); [[https://www.rcsb.org/structure/5JP1|5JP1]], [[https://www.rcsb.org/structure/5JP3|5JP3]] ( Pruneda //et al.//, 2016 )+GenBank ID: [[https://www.ncbi.nlm.nih.gov/protein/DAA34040.1|DAA34040.1]] (760 aa; new structural annotation)\\ 
 +RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_228949438.1|WP_228949438.1]] (760 aa; new structural annotation)\\ 
 +3D structure: [[https://www.rcsb.org/structure/2OIV|2OIV]], [[https://www.rcsb.org/structure/2OIX|2OIX]] (Chosed //et al//., 2007); [[https://www.rcsb.org/structure/5JP1|5JP1]], [[https://www.rcsb.org/structure/5JP3|5JP3]] (Pruneda //et al.//, 2016) 
 ===== Biological function ===== ===== Biological function =====
  
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 === Regulation === === Regulation ===
  
-The //xopD// gene expression is induced in a //hrpG//- and //hrpX//-dependent manner (Noël //et al//., 2002). It was described that, XopD promoter does not contain a PIP box, but a //hrp// box, which is found in all //hrpL//-dependent promoters in //P.syringae// and //Erwinia// spp. (GGAACTNA-N13-CGACNNA; consensus: GGAACcNa-N13/14-cCACNNA) (Noël //et al//., 2002; Innes //et al//., 1993). However, after carefully inspected the intergenic region of the //Xanthomonas euvesicatoria// pv. //euvesicatoria// 85-10 genome (Xcv 85-10) between the //XCV0436// locus and the //xopD// locus for an alternative promoter and start site (Kim //et al//., 2011), identified a putative PIP box and ATG just downstream of the //XCV0436// locus. Using ATG as the putative start codon, the respective //xopD// ORF predicts a protein with 760 aa with a longer N-terminal domain (Kim //et al//., 2011).+The //xopD// gene expression is induced in a //hrpG//- and //hrpX//-dependent manner (Noël //et al//., 2002). It was described that, XopD promoter does not contain a PIP box, but a //hrp// box, which is found in all //hrpL//-dependent promoters in //P. syringae// and //Erwinia// spp. (GGAACTNA-N13-CGACNNA; consensus: GGAACcNa-N13/14-cCACNNA) (Noël //et al//., 2002; Innes //et al//., 1993). However, after carefully inspected the intergenic region of the //Xanthomonas euvesicatoria// pv. //euvesicatoria// 85-10 genome (Xcv 85-10) between the //XCV0436// locus and the //xopD// locus for an alternative promoter and start site (Kim //et al//., 2011), identified a putative PIP box and ATG just downstream of the //XCV0436// locus. Using ATG as the putative start codon, the respective //xopD// ORF predicts a protein with 760 aa with a longer N-terminal domain (Kim //et al//., 2011).
 === Phenotypes === === Phenotypes ===
  
 XopD is a unique virulence factor that promotes tolerance to //Xcv// 85-10 in infected host leaves and affects bacteria miltiplication (Kim //et al//., 2008). It was found that delays the onset leaf chlorosis and necrosis, two phenotypes associated with pathogen-triggered immunity (PTI) activation (Kim //et al//., 2008). Delaying in tissue damages and lower chlorophyll loss corelate with reduced host defense transcription and reduced salicylic acid (SA) levels-plant defense hormone that limits the spread of pathogens in infected host plant. Moreover, expression of XopD //in planta// is sufficient to repress not only SA- but also jasmonic acid–induced gene transcription (Hotson //et al//., 2003; Kim //et al//., 2008; Kim //et al//., 2011). It was also shown that XopD highly induces the tomato transcription factor, bHLH132 (Kim //et al//., 2019). This induction is dependant of XopD SUMO protease activity. This sutdy has shown that is involved in both plant development and plant defense regulation and that silencing bHLH132 mRNA expression results in stuned tomato with enhanced susceptibility to //Xcv// infection. XopD is a unique virulence factor that promotes tolerance to //Xcv// 85-10 in infected host leaves and affects bacteria miltiplication (Kim //et al//., 2008). It was found that delays the onset leaf chlorosis and necrosis, two phenotypes associated with pathogen-triggered immunity (PTI) activation (Kim //et al//., 2008). Delaying in tissue damages and lower chlorophyll loss corelate with reduced host defense transcription and reduced salicylic acid (SA) levels-plant defense hormone that limits the spread of pathogens in infected host plant. Moreover, expression of XopD //in planta// is sufficient to repress not only SA- but also jasmonic acid–induced gene transcription (Hotson //et al//., 2003; Kim //et al//., 2008; Kim //et al//., 2011). It was also shown that XopD highly induces the tomato transcription factor, bHLH132 (Kim //et al//., 2019). This induction is dependant of XopD SUMO protease activity. This sutdy has shown that is involved in both plant development and plant defense regulation and that silencing bHLH132 mRNA expression results in stuned tomato with enhanced susceptibility to //Xcv// infection.
  
-For instance, XcvΔ//xopD// mutants grow poorly in infected tomato leaves because defenses dependent from SA were not stifled (Kim //et al//., 2008). It is also known that XopD<sub>Xcv85-10</sub> directly interacts with tomato ethylene responsive transcription factor SlERF4. XopD desumoylates SlERF4 and suppress its activity in ethylene production, which is required for anti-Xcv ethylene stimulated immunity and symptom development (Kim //et al//., 2013). XopD<sub>XccB100</sub> from the// Xanthomonas campestris// pv. //campestris// (//Xcc//) strain B100 specifically interacts with MYB30 to suppress its activity in activating plant defense responses required for anti-//Xcc// immunity (Canonne //et al//., 2011).+For instance, XcvΔ//xopD// mutants grow poorly in infected tomato leaves because defenses dependent from SA were not stifled (Kim //et al//., 2008). It is also known that XopD<sub>Xcv85-10</sub> directly interacts with tomato ethylene responsive transcription factor SlERF4. XopD desumoylates SlERF4 and suppress its activity in ethylene production, which is required for anti-Xcv ethylene stimulated immunity and symptom development (Kim //et al//., 2013). XopD<sub>XccB100</sub> from the //Xanthomonas campestris// pv. //campestris// (//Xcc//) strain B100 specifically interacts with MYB30 to suppress its activity in activating plant defense responses required for anti-//Xcc// immunity (Canonne //et al//., 2011).
  
 Comparative analysis of the XopD effector family in other phytopathogenic bacteria revealed that so called XopD-like proteins presents differences in sequence and length of their N-terminal domains. This suggests that the N-terminal domain of XopD and XopD-like effectors might impart substrate and/or host specificity. Comparative analysis of the XopD effector family in other phytopathogenic bacteria revealed that so called XopD-like proteins presents differences in sequence and length of their N-terminal domains. This suggests that the N-terminal domain of XopD and XopD-like effectors might impart substrate and/or host specificity.
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 === Enzymatic function === === Enzymatic function ===
  
-Peptidase, isopeptidase or desumoylating enzyme (Hotson// et al//., 2003).+Peptidase, isopeptidase or desumoylating enzyme (Hotson //et al//., 2003).
 === Interaction partners === === Interaction partners ===
  
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 === In xanthomonads === === In xanthomonads ===
  
-Yes (e.g. //Xanthomonas campestris// pv. //vesicatoria//, //X. campestris// pv. //campestris// (Kim //et al//., 2011).+Yes (//e.g.//, //Xanthomonas campestris// pv. //vesicatoria//, //X. campestris// pv. //campestris// (Kim //et al//., 2011).
 === In other plant pathogens/symbionts === === In other plant pathogens/symbionts ===
  
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 Tan L, Rong W, Luo H, Chen Y, He C (2014). The //Xanthomonas campestris// effector protein XopD<sub>Xcc8004</sub> triggers plant disease tolerance by targeting DELLA proteins. New Phytol. 204: 595-608. DOI: [[https://doi.org/10.1111/nph.12918|10.1111/nph.12918]] Tan L, Rong W, Luo H, Chen Y, He C (2014). The //Xanthomonas campestris// effector protein XopD<sub>Xcc8004</sub> triggers plant disease tolerance by targeting DELLA proteins. New Phytol. 204: 595-608. DOI: [[https://doi.org/10.1111/nph.12918|10.1111/nph.12918]]
 +
 +===== Acknowledgements =====
 +
 +This fact sheet is based upon work from COST Action CA16107 EuroXanth, supported by COST (European Cooperation in Science and Technology).
  
bacteria/t3e/xopd.1594225642.txt.gz · Last modified: 2023/01/09 10:20 (external edit)

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