Type III effector proteins from the plant pathogen Xanthomonas and their role in the interaction with the host plant

Gürlebeck, Doreen; Thieme, Frank; Bonas, Ulla

doi:10.1016/j.jplph.2005.11.011

Cited by 167 publications

(152 citation statements)

References 205 publications

(281 reference statements)

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“…Xcv enters the leaf via wounds or natural openings created by guard cells and hydrathodes. Once in the apoplast, Xcv becomes infectious and uses the type III secretion (T3S) apparatus to secrete and translocate effector proteins into plant cells (Gurlebeck et al, 2006). Mutant bacteria deficient in T3S or lacking T3S proteins are less pathogenic or nonpathogenic.…”

Section: Introductionmentioning

confidence: 99%

“…Bioinformatics and functional genetic screens have been used to identify and characterize the T3S effector proteome in the genome of Xcv 85-10, a model strain used to study bacterial spot (Roden et al, 2004a;Thieme et al, 2005;Gurlebeck et al, 2006). Although numerous effectors (>30) have been identified (Gurlebeck et al, 2006), the biochemical function of these proteins in promoting bacterial colonization within the host, resulting in either disease or resistance signaling, is poorly understood.…”

Section: Introductionmentioning

confidence: 99%

“…Although numerous effectors (>30) have been identified (Gurlebeck et al, 2006), the biochemical function of these proteins in promoting bacterial colonization within the host, resulting in either disease or resistance signaling, is poorly understood. Yet, a central theme emerging from the study of different phytopathogenic strains indicates that bacteria deliberately suppress plant immune responses to interfere with the activation of disease resistance protein-mediated pathways (reviewed in Mudgett, 2005).…”

Section: Introductionmentioning

confidence: 99%

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A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

et al. 2007

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AvrBsT is a type III effector from Xanthomonas campestris pv vesicatoria that is translocated into plant cells during infection. AvrBsT is predicted to encode a Cys protease that targets intracellular host proteins. To dissect AvrBsT function and recognition in Arabidopsis thaliana, 71 ecotypes were screened to identify lines that elicit an AvrBsT-dependent hypersensitive response (HR) after Xanthomonas campestris pv campestris (Xcc) infection. The HR was observed only in the Pi-0 ecotype infected with Xcc strain 8004 expressing AvrBsT. To create a robust pathosystem to study AvrBsT immunity in Arabidopsis, the foliar pathogen Pseudomonas syringae pv tomato (Pst) strain DC3000 was engineered to translocate AvrBsT into Arabidopsis by the Pseudomonas type III secretion (T3S) system. Pi-0 leaves infected with Pst DC3000 expressing a Pst T3S signal fused to AvrBsT-HA (AvrBsT HYB -HA) elicited HR and limited pathogen growth, confirming that the HR leads to defense. Resistance in Pi-0 is caused by a recessive mutation predicted to inactivate a carboxylesterase known to hydrolyze lysophospholipids and acylated proteins in eukaryotes. Transgenic Pi-0 plants expressing the wild-type Columbia allele are susceptible to Pst DC3000 AvrBsT HYB -HA infection. Furthermore, wild-type recombinant protein cleaves synthetic p-nitrophenyl ester substrates in vitro. These data indicate that the carboxylesterase inhibits AvrBsT-triggered phenotypes in Arabidopsis. Here, we present the cloning and characterization of the SUPPRESSOR OF AVRBST-ELICITED RESISTANCE1.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

et al. 2007

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“…Seventeen effectors have been confirmed in Xcv [71], with only a few characterized for molecular or biochemical function. Several members of the YopJ/AvrRxv family of effectors have been shown to use a catalytic triad to target host proteins [8,13,22,25].…”

Section: Discussionmentioning

confidence: 99%

Identification of a host 14-3-3 protein that interacts with Xanthomonas effector AvrRxv

Whalen

Richter

Zakhareyvich

et al. 2008

Physiological and Molecular Plant Pathology

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AvrRxv is a member of a family of pathogen effectors present in pathogens of both plant and mammalian species. Xanthomonas campestris pv. vesicatoria strains carrying AvrRxv induce a hypersensitive response (HR) in the tomato cultivar Hawaii 7998. Using a yeast two-hybrid screen, we identified a 14-3-3 protein from tomato that interacts with AvrRxv called AvrRxv Interactor 1 (ARI1). The interaction was confirmed in vitro with affinity chromatography. Using mutagenesis, we identified a 14-3-3-binding domain in AvrRxv and demonstrated that a mutant in that domain showed concomitant loss of interaction with ARI1 and HR-inducing activity in tomato. These results demonstrate that the AvrRxv bacterial effector recruits 14-3-3 proteins for its function within host cells. AvrRxv homologues YopP and YopJ from Yersinia do not have AvrRxv-specific HR-inducing activity when delivered into tomato host cells by Agrobacterium. Although YopP itself cannot induce HR, its C-terminal domain containing the catalytic residues can replace that of AvrRxv in an AvrRxv-YopP chimera for HR-inducing activity. Phylogenetic analysis indicates that the sequences encoding the C-termini of family members are evolving independently from those encoding the N-termini. Our results support a model in which there are three functional domains in proteins of the family, translocation, interaction, and catalytic.

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“…Another criterion used to identify putative effectors from obligate intracellular pathogens has been the presence of nuclear localization domains, which allows effectors to directly modulate plant gene expression [58,59]. For many years, effectors capable of migrating to the plant cell nucleus have only been described in bacteria [58–60], but more recently these motifs together with nuclear localization of effectors has been described in fungi [61,62] and nematodes [63]. In bioinformatics pipelines designed to identify putative effectors, the inclusion of steps to remove proteins containing subcellular localization signals will remove these effectors, although researchers could analyze these amino acid sequences directly using the online tool TargetP 1.1 Server (http://www.cbs.dtu.dk/services/TargetP).…”

Section: Where and How To Look For Effectors?mentioning

confidence: 99%

Identification of Plasmodiophora brassicae effectors — A challenging goal

et al. 2018

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Clubroot is an economically important disease affecting Brassica plants worldwide. Plasmodiophora brassicae is the protist pathogen associated with the disease, and its soil-borne obligate parasitic nature has impeded studies related to its biology and the mechanisms involved in its infection of the plant host. The identification of effector proteins is key to understanding how the pathogen manipulates the plant’s immune response and the genes involved in resistance. After more than 140 years studying clubroot and P. brassicae, very little is known about the effectors playing key roles in the infection process and subsequent disease progression. Here we analyze the information available for identified effectors and suggest several features of effector genes that can be used in the search for others. Based on the information presented in this review, we propose a comprehensive bioinformatics pipeline for effector identification and provide a list of the bioinformatics tools available for such.

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Type III effector proteins from the plant pathogen Xanthomonas and their role in the interaction with the host plant

Cited by 167 publications

References 205 publications

A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

Identification of a host 14-3-3 protein that interacts with Xanthomonas effector AvrRxv

Identification of Plasmodiophora brassicae effectors — A challenging goal

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