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bacteria:t3e:xopb [2023/05/17 12:39] – [XopB] rkoebnikbacteria:t3e:xopb [2025/07/04 23:22] (current) – jfpothier
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-====== XopB ======+====== The Type III Effector XopB from //Xanthomonas// ======
  
 Author: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]]\\ Author: [[https://www.researchgate.net/profile/Ralf_Koebnik|Ralf Koebnik]]\\
 Internal reviewer: [[https://www.researchgate.net/profile/Nay_Dia|Nay C. Dia]]\\ Internal reviewer: [[https://www.researchgate.net/profile/Nay_Dia|Nay C. Dia]]\\
-Expert reviewer: FIXME 
  
 Class: XopB\\ Class: XopB\\
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 XopB was discovered in a cDNA-AFLP screen (Noël //et al.//, 2001). XopB was discovered in a cDNA-AFLP screen (Noël //et al.//, 2001).
 +
 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
 A chimeric protein consisting of a C-terminally truncated XopB where the last 52 residues (5 kDa) were replaced by the triple c-myc epitope (5 kDa) was secreted into culture supernatants of a strain with a constitutively active form of //hrpG// in a type III secretion-dependent manner (Noël //et al.//, 2001). XopB belongs to translocation class B (Schulze //et al.//, 2012). Mutation studies of a putative translocation motif (TrM) showed that the proline/arginine-rich motif is required for efficient type III-dependent secretion and translocation of XopB and determines the dependence of XopB transport on the general T3S chaperone HpaB (Prochaska //et al.//, 2018). A chimeric protein consisting of a C-terminally truncated XopB where the last 52 residues (5 kDa) were replaced by the triple c-myc epitope (5 kDa) was secreted into culture supernatants of a strain with a constitutively active form of //hrpG// in a type III secretion-dependent manner (Noël //et al.//, 2001). XopB belongs to translocation class B (Schulze //et al.//, 2012). Mutation studies of a putative translocation motif (TrM) showed that the proline/arginine-rich motif is required for efficient type III-dependent secretion and translocation of XopB and determines the dependence of XopB transport on the general T3S chaperone HpaB (Prochaska //et al.//, 2018).
 +
 === Regulation === === Regulation ===
  
 The //xopB// gene was shown to be expressed in a //hrpG//- and //hrpX//-dependent manner (Noël //et al.//, 2001). Presence of a PIP and ‐10 box (TTCGB‐N<sub>15</sub> ‐TTCGB‐N<sub>30–32</sub> ‐YANNNT) (Schulze //et al.//, 2012). The //xopB// gene was shown to be expressed in a //hrpG//- and //hrpX//-dependent manner (Noël //et al.//, 2001). Presence of a PIP and ‐10 box (TTCGB‐N<sub>15</sub> ‐TTCGB‐N<sub>30–32</sub> ‐YANNNT) (Schulze //et al.//, 2012).
 +
 === Phenotypes === === Phenotypes ===
  
 A deletion of //xopB// did not affect pathogenicity or bacterial growth in plants (Noël //et al.//, 2001). Later it was found that XopB contributes to disease symptoms and bacterial growth (Schulze //et al.//, 2012; Priller //et al.//, 2016). Infection of susceptible pepper plants with a strain lacking //xopB// resulted in increased formation of salicylic acid (SA) and expression of pathogenesis-related (PR) genes (Priller //et al.//, 2016). When expressed in yeast, XopB attenuated cell proliferation (Salomon //et al.//, 2011). XopB caused a fast and confluent cell death when transiently expressed in the non-host //Nicotiana benthamiana// leaves, whereas its expression in host tomato leaves did not result in a visible phenotype, even seven days after agroinfiltration (Salomon //et al.//, 2011). XopB suppresses pathogen‐associated molecular pattern (PAMP)‐triggered plant defense gene expression and inhibits cell death reactions induced by different T3Es, thus suppressing defense responses related to both PAMP‐triggered immunity (PTI) and effector‐triggered immunity (ETI) (Schulze //et al.//, 2012). For instance, XopB inhibited the flg22-triggered burst of reactive oxygen species (ROS) (Priller //et al.//, 2016). Interestingly, a XopB point mutant derivative was defective in the suppression of ETI‐related responses, but still interfered with vesicle trafficking and was only slightly affected with regard to the suppression of defense gene induction, suggesting that XopB‐mediated suppression of PTI and ETI is dependent on different mechanisms that can be functionally separated (Schulze //et al.//, 2012). A deletion of //xopB// caused a prominent increase in cell wall-bound invertase activity, which might be linked to defense responses because an increase in the apoplastic hexose-to-sucrose ratio has been suggested to strengthen plant defense (Sonnewald //et al.//, 2012). Expression of //xopB// in //Arabidopsis thaliana// promoted the growth of the virulent //Pseudomonas syringae// pv. //tomato// DC3000 strain, which was paralleled by a decreased salicylic acid (SA)-pool and a lower induction of SA-dependent pathogenicity-related (PR) gene expression (Priller //et al.//, 2016). A deletion of //xopB// did not affect pathogenicity or bacterial growth in plants (Noël //et al.//, 2001). Later it was found that XopB contributes to disease symptoms and bacterial growth (Schulze //et al.//, 2012; Priller //et al.//, 2016). Infection of susceptible pepper plants with a strain lacking //xopB// resulted in increased formation of salicylic acid (SA) and expression of pathogenesis-related (PR) genes (Priller //et al.//, 2016). When expressed in yeast, XopB attenuated cell proliferation (Salomon //et al.//, 2011). XopB caused a fast and confluent cell death when transiently expressed in the non-host //Nicotiana benthamiana// leaves, whereas its expression in host tomato leaves did not result in a visible phenotype, even seven days after agroinfiltration (Salomon //et al.//, 2011). XopB suppresses pathogen‐associated molecular pattern (PAMP)‐triggered plant defense gene expression and inhibits cell death reactions induced by different T3Es, thus suppressing defense responses related to both PAMP‐triggered immunity (PTI) and effector‐triggered immunity (ETI) (Schulze //et al.//, 2012). For instance, XopB inhibited the flg22-triggered burst of reactive oxygen species (ROS) (Priller //et al.//, 2016). Interestingly, a XopB point mutant derivative was defective in the suppression of ETI‐related responses, but still interfered with vesicle trafficking and was only slightly affected with regard to the suppression of defense gene induction, suggesting that XopB‐mediated suppression of PTI and ETI is dependent on different mechanisms that can be functionally separated (Schulze //et al.//, 2012). A deletion of //xopB// caused a prominent increase in cell wall-bound invertase activity, which might be linked to defense responses because an increase in the apoplastic hexose-to-sucrose ratio has been suggested to strengthen plant defense (Sonnewald //et al.//, 2012). Expression of //xopB// in //Arabidopsis thaliana// promoted the growth of the virulent //Pseudomonas syringae// pv. //tomato// DC3000 strain, which was paralleled by a decreased salicylic acid (SA)-pool and a lower induction of SA-dependent pathogenicity-related (PR) gene expression (Priller //et al.//, 2016).
 +
 === Localization === === Localization ===
  
 XopB localizes to the Golgi apparatus and cytoplasm of the plant cell and interferes with eukaryotic vesicle trafficking (Schulze //et al.//, 2012). Interestingly, a short ORF is found between the PIP box/-10 promoter region and the predicted translation start codon of //xopB// in Xcv<sub>85-10</sub>, which encodes a 25-aa peptide (MGLCSSKPRVQAQLNIMRPRHRAD) with a strong palmitoylation signal (Koebnik, unpublished). Whether this peptide once belonged to XopB or to another candidate effector, if at all, remains unknown. XopB localizes to the Golgi apparatus and cytoplasm of the plant cell and interferes with eukaryotic vesicle trafficking (Schulze //et al.//, 2012). Interestingly, a short ORF is found between the PIP box/-10 promoter region and the predicted translation start codon of //xopB// in Xcv<sub>85-10</sub>, which encodes a 25-aa peptide (MGLCSSKPRVQAQLNIMRPRHRAD) with a strong palmitoylation signal (Koebnik, unpublished). Whether this peptide once belonged to XopB or to another candidate effector, if at all, remains unknown.
 +
 === Enzymatic function === === Enzymatic function ===
  
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 === In xanthomonads === === In xanthomonads ===
  
-Yes (e.g., //X. fragariae//, //X. cynarae// pv. //gardneri// (syn. //X. gardneri//), //X. oryzae//, //X. vasicola//) (Harrison //et al.//, 2014).+Yes (//e.g.//, //X. fragariae//, //X. cynarae// pv. //gardneri// (syn. //X. gardneri//), //X. oryzae//, //X. vasicola//) (Harrison //et al.//, 2014). 
 === In other plant pathogens/symbionts === === In other plant pathogens/symbionts ===
  
-Yes (e.g., //Pseudomonas// spp., //Ralstonia solanacearum//, //Acidovorax// spp., //Pantoea agglomerans//) (Schulze //et al.//, 2012).+Yes (//e.g.//, //Pseudomonas// spp., //Ralstonia solanacearum//, //Acidovorax// spp., //Pantoea agglomerans//) (Schulze //et al.//, 2012). 
 ===== References ===== ===== References =====
  
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 Sonnewald S, Priller JPR, Schuster J, Glickmann E, Hajirezaei MR, Siebig S, Mudgett MB, Sonnewald U (2012). Regulation of cell wall-bound invertase in pepper leaves by //Xanthomonas campestris// pv. //vesicatoria// type three effectors. PLoS One 7: e51763. DOI: [[https://doi.org/10.1371/journal.pone.0051763|10.1371/journal.pone.0051763]] Sonnewald S, Priller JPR, Schuster J, Glickmann E, Hajirezaei MR, Siebig S, Mudgett MB, Sonnewald U (2012). Regulation of cell wall-bound invertase in pepper leaves by //Xanthomonas campestris// pv. //vesicatoria// type three effectors. PLoS One 7: e51763. DOI: [[https://doi.org/10.1371/journal.pone.0051763|10.1371/journal.pone.0051763]]
 +
 +===== Acknowledgements =====
 +
 +This fact sheet is based upon work from COST Action CA16107 EuroXanth, supported by COST (European Cooperation in Science and Technology).
  
bacteria/t3e/xopb.1684323583.txt.gz · Last modified: 2023/05/17 12:39 by rkoebnik

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