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PubMed2006

Targeting of two effector protein classes to the type III secretion system by a HpaC- and HpaB-dependent protein complex from Xanthomonas campestris pv. vesicatoria.

The Gram-negative plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria translocates effector proteins via a specialized type III secretion (TTS) system into the host cell cytosol. The efficient secretion of many effector proteins depends on the global TTS chaperone HpaB. Here, we identified a novel export control protein, HpaC, which significantly contributes to bacterial pathogenicity. Deletion of hpaC leads to a severe reduction in secretion of effector proteins and the putative type III translocon proteins HrpF and XopA. By contrast, secretion of the TTS pilus protein HrpE is not affected. We provide experimental evidence that HpaC differentiates between two classes of effector proteins. Using an in vivo reporter assay, we found that HpaC specifically promotes the translocation of the effector proteins XopJ and XopF1 into the plant cell, whereas AvrBs3 and XopC are efficiently translocated even in the absence of HpaC. Similar findings were obtained for HpaB. Inhibition of protein synthesis suggests that HpaB is involved in the secretion of stored effector proteins. Furthermore, protein-protein interaction studies revealed that HpaB and HpaC form an oligomeric protein complex and that they interact with members of both effector protein classes and the conserved TTS system component HrcV. Taken together, our data indicate that HpaB and HpaC play a central role in recruiting TTS substrates to the secretion apparatus.

Bacterial Proteins↗

PubMed1997

Immunodominant and subdominant CTL responses to Listeria monocytogenes infection.

Protective immunity to infection by intracellular pathogens begins with expansion of Ag-specific, effector T lymphocytes and is followed by persistence of pathogen-specific memory T cells. Infection by Listeria monocytogenes, an intracellular bacterium, induces cytolytic T lymphocytes that mediate systemic sterilization and long term immunity. In cells infected with L. monocytogenes, H2-Kd class I molecules present three nonamer peptides, listeriolysin (LLO) 91-99, p60 217-225, and p60 449-457, to CTL. Herein we show that during the peak CTL response to L. monocytogenes infection, the ratio of T cells specific for LLO 91-99, p60 217-225, and p60 449-457 is approximately 20:10:1, respectively. While the number of Ag-specific T lymphocytes decreases in the weeks after infection, the proportion of T lymphocytes specific for the three epitopes is maintained. Repertoire analysis of a subset of L. monocytogenes-specific T cells, using alanine-substituted variants of p60 217-225, indicates that the range of T cell specificities is maintained by memory cells. These results indicate that the breadth and relative magnitude of T cell specificities initially elicited by an infection are transmitted to the memory compartment. Our results suggest that T lymphocytes with different gross and fine Ag specificities are equally likely to become memory T cells.

Acute Disease↗

PubMed1999

Construction of a gene probe for detection of P virus (Reoviridae) in a marine decapod.

The construction is described of a molecular probe to P virus, a double stranded RNA virus belonging to the Reoviridiae, which is an endemic pathogen of swimming crabs in British coastal waters and the Mediterranean. The probe hybridises to the P virus genome and can be easily produced in large quantities by PCR. It may be used by dot blotting or in situ hybridisation to specifically detect P virus in tissues and cells of natural or experimentally infected animals. Analyses of tissue samples with this probe show that the virus infects connective tissues of gills and hepatopancreas. This is the first gene probe to be constructed for a native viral pathogen of temperate water brachyurans and it will be useful to study virus ecology and virus-host interactions in vivo and in vitro. An understanding of these processes is essential to control and manage disease and, ultimately, to identify immune effectors capable of destroying viral pathogens.

Animals↗

PubMed2005

Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ.

The type III secretion system (TTSS) is a macromolecular structure that spans the cell wall of Gram-negative bacterial pathogens, enabling delivery of virulence effector proteins directly to the membranes and cytosol of host eukaryotic cells. TTSS consists of a conserved needle complex (NC) that is composed of sets of inner and outer membranes rings connected by a periplasmic rod. Enteropathogenic Escherichia coli (EPEC) is an extracellular diarrhoeagenic pathogen that uses TTSS to induce actin polymerization and colonizes the intestinal epithelium. In EPEC, EscJ is predicted to be targeted to the periplasm, in a sec-dependent manner, and to bridge the TTSS membrane-associated rings. In this study we determined the global fold of EscJ using Nuclear Magnetic Resonance spectroscopy. We show that EscJ comprises two subdomains (D1 - amino acid residues 1-55 in the mature protein, and D2 - amino acid residues 90-170), each comprising a three-stranded beta-sheet flanked by two alpha-helices. A flexible region (residues 60-85) couples the structured regions D1 and D2. Periplasmic overexpression of EscJ(D1) and EscJ(D2) in a single escJ mutant bacterium failed to restore protein secretion activity, suggesting that the flexible linker is essential for the rod function. In contrast, periplasmic overexpression of EscJ(D1) and EscJ(D2) in the same wild-type bacterium had a dominant-negative phenotype suggesting defective assembly of the TTSS and protein translocation.

Amino Acid Sequence↗

PubMed2004

The anatomy of mucosal immune responses.

It remains unclear how and where unresponsiveness to fed antigens is induced. This "oral tolerance" is probably necessary to prevent the array of immune effector mechanisms required to counteract pathogens of the mucosae from being misdirected against food antigens or commensal flora. It will obviously be important to dissect where, when, and how such immunological homeostasis is maintained in the gut, but it will also be necessary to determine whether similar inductive and effector mechanisms are required for the therapeutic applications of oral tolerance systemically. This may be influenced by anatomical and microenvironmental effects on the phenotype and/or activation state of the antigen-presenting cell (APC), which presents orally delivered antigen. Fed antigen passes from the intestinal lumen either via the villus epithelium and M cells in the Peyer's patches (PP) or the mucosal lamina propria to the organized lymphoid tissues of the PP and mesenteric lymph nodes (MLN). In addition, there is evidence that mucosally administered antigen also gains access directly to peripheral lymphoid organs. Each of these sites contains distinctive populations of APCs and has unique local microenvironments that may influence the immune response in different ways. We propose that feeding antigen in high doses may induce clonal anergy, deletion, or altered differentiation because it gains direct access to resting APCs in the T cell areas of both the gut-associated lymphoid tissues (GALT) and peripheral lymphoid organs, with presentation occurring in the absence of productive costimulation. By contrast, low doses of tolerizing antigen may be taken up and presented preferentially by APCs in the GALT, where the local environment may favor the induction of regulatory T cells. This is consistent with our own and others findings, using adoptive transfer of TcR tg T cells. These studies have shown that antigen-specific CD4(+) T cells are activated simultaneously in all peripheral and gut-associated lymphoid organs after feeding high doses of proteins, but that this may be more restricted to local tissues when lower doses are used. Another level of anatomical control is imposed within lymphoid organs, where migration of T cells through distinct anatomical compartments can affect their differentiation. We find that, in contrast to orally primed T cells, orally tolerized T cells are unable to migrate into B cell follicles during their initial exposure to antigen. This affects their differentiation as upon subsequent challenge with antigen in adjuvant, tolerized T cells can be found in follicles but are unable to provide the B cell help that primed T cells can deliver. We hypothesize that the initial defective migration of tolerized T cells prevents them from receiving signals from antigen-specific B cells in follicles and results in abortive differentiation. Thus, both gross and fine anatomical location of fed antigen presentation may be important in mucosal immunoregulation.

Animals↗

PubMed2003

Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance.

Type III pili deliver effector proteins (virulence factors) from bacterial pathogens to host cells. Plants express disease resistance (R) proteins that respond specifically to a particular type III effector by activating immune responses. We demonstrated previously that two unrelated type III effectors from Pseudomonas syringae target and modify the Arabidopsis RIN4 protein. Here, we show that AvrRpt2, a third, unrelated type III effector, also targets RIN4 and induces its posttranscriptional disappearance. This effect is independent of the presence of RPS2, the Arabidopsis R protein that senses AvrRpt2. RIN4 overexpression inhibits multiple phenotypes associated with AvrRpt2 function. Conversely, disruption of RIN4 results in RPS2-dependent lethality. RPS2 and RIN4 physically associate in the plant. We suggest that RIN4 is the target of the AvrRpt2 virulence function, and that perturbation of RIN4 activates RPS2. Thus, RIN4 is a point of convergence for the activity of at least three unrelated P. syringae type III effectors.

Arabidopsis↗

PubMed2005

The bacterial injection kit: type III secretion systems.

Type III secretion (T3S) systems are widespread among Gram-negative bacteria pathogenic for animals and plants, including Yersinia spp., Salmonella spp., Shigella spp., enteropathogenic Escherichia coli, enterohaemorrhagic E. coli, or Pseudomonas spp. T3S systems allow bacteria to inject virulence proteins, called T3S effectors, into the cytosol of their eukaryotic host cells. These virulence factors will paralyze or reprogram the eukaryotic cell to the benefit of the pathogen. T3S effectors display a large repertoire of biochemical activities and modulate the function of crucial host regulatory molecules such as small guanosine triphosphate (GTP)-binding proteins, mitogen-activated protein kinases (MAPKs), nuclear factor (NF)-kappaB, or phosphoinositides. The activity of T3S effectors allows bacteria, for example, to invade non-phagocytic cells or to inhibit phagocytosis, to downregulate or promote pro-inflammatory responses, to induce apoptosis, to prevent autophagy, or to modulate intracellular trafficking. In this review, we present the most recent advances in the understanding of the mode of action of T3S effectors. We highlight the biochemical activities of these eukaryotic-like bacterial proteins that are shared among pathogens carrying T3S systems and the sequence, structural and functional resemblances between T3S effectors and eukaryotic proteins.

Animals↗

PubMed1983

[Significance of immunologic effector mechanisms in infectious endocarditis].

Whereas a number of investigations deals with extracardiac manifestations of immune reactions in infective endocarditis (e.g. circulating immune complexes), immunological effector mechanisms directed against the heart itself have not yet been analyzed. In 72 patients with infective endocarditis (41 patients with defined pathogen, 31 no pathogen isolated) humoral und cellular immunological effector mechanisms were investigated. Antibodies directed against the cytoskeleton of myocardial cells and against the endocardium were demonstrated in 60% to 100% depending on the infective pathogen and the clinical course. Whereas the antibodies were found in subacute and chronic courses regularly, they were found less frequently in acute lethal cases. Antibodies directed against connective tissue, endocardium and sarcolemma were indicative of, but not specific for the endocardial affection. Those antibodies which were directed against the inner parts of the sarcolemma, the myolemma, appear to be indicators of an additional myocardial affection, if they are cytolytic against vital cardiocytes in vitro. Circulating immune complexes are non-specific markers of an increased immunoreactivity. They were detected in 35 out of 41 patients with defined bacterial pathogen in the early phase of the disease. Both, their incidence and serum concentrations decreased significantly after antibiotic treatment. Cellular immune reactions directed against vital heart cells (e.g. cytotoxic reactions) can most likely be attributed to K- or NK-lymphocytes and were found in 48% of patients. Serum factors such as circulating immune complexes and/or antimyolemmal antibodies may enhance or block this cytotoxic reaction.

Adult↗

PubMed2004

A family of conserved bacterial effectors inhibits salicylic acid-mediated basal immunity and promotes disease necrosis in plants.

Salicylic acid (SA)-mediated host immunity plays a central role in combating microbial pathogens in plants. Inactivation of SA-mediated immunity, therefore, would be a critical step in the evolution of a successful plant pathogen. It is known that mutations in conserved effector loci (CEL) in the plant pathogens Pseudomonas syringae (the Delta CEL mutation), Erwinia amylovora (the dspA/E mutation), and Pantoea stewartii subsp. stewartii (the wtsE mutation) exert particularly strong negative effects on bacterial virulence in their host plants by unknown mechanisms. We found that the loss of virulence in Delta CEL and dspA/E mutants was linked to their inability to suppress cell wall-based defenses and to cause normal disease necrosis in Arabidopsis and apple host plants. The Delta CEL mutant activated SA-dependent callose deposition in wild-type Arabidopsis but failed to elicit high levels of callose-associated defense in Arabidopsis plants blocked in SA accumulation or synthesis. This mutant also multiplied more aggressively in SA-deficient plants than in wild-type plants. The hopPtoM and avrE genes in the CEL of P. syringae were found to encode suppressors of this SA-dependent basal defense. The widespread conservation of the HopPtoM and AvrE families of effectors in various bacteria suggests that suppression of SA-dependent basal immunity and promotion of host cell death are important virulence strategies for bacterial infection of plants.

Arabidopsis↗

PubMed2006

Modulation of phosphoinositide metabolism by pathogenic bacteria.

Phosphoinositide metabolism plays a pivotal role in the regulation of receptor-mediated signal transduction, actin remodelling and membrane dynamics. Phosphoinositides co-ordinate these processes by recruiting protein effectors to distinct cellular membranes in a time- and organelle-dependent manner. Intracellular bacterial pathogens interfere with phosphoinositide metabolism to direct their entry into eukaryotic cells, form replication-permissive vacuoles, modulate apoptosis, or trigger fluid secretion. Gram-negative pathogens such as Legionella pneumophila, Shigella flexneri, or Salmonella enterica employ secretion systems to invade host cells by 'pathogen-triggered phagocytosis' and thereby bypass a requirement for phosphatidylinositol 3-kinases [PI(3)Ks]. Contrarily, 'receptor-mediated phagocytosis' of Yersinia spp., Listeria monocytogenes and other pathogenic bacteria depends on PI(3)Ks. Secreted effector proteins have been found to directly bind to and modify host cell phosphoinositides, thus modulating phagocytosis and intracellular survival of the pathogens. These effectors include L. pneumophila proteins that specifically attach to phosphatidylinositol 4-phosphate [PI(4)P] on the Legionella-containing vacuole, and phosphoinositide phosphatases produced by S. flexneri, S. enterica or Mycobacterium tuberculosis. This review covers current knowledge about subversion of host cell phosphoinositide metabolism by intracellular bacterial pathogens with an emphasis on recently identified secreted effector proteins directly engaging phosphoinositides.

Animals↗

PubMed1996

Soluble invasion plasmid antigen C (IpaC) from Shigella flexneri elicits epithelial cell responses related to pathogen invasion.

Shigella flexneri invades colonic epithelial cells by pathogen-induced phagocytosis. The three proposed effectors of S. flexneri internalization are invasion plasmid antigens B (IpaB), IpaC, and IpaD, which are encoded on the pathogen's 230-kb virulence plasmid and translocated to the extracellular milieu via the Mxi-Spa translocon. To date, there are no definitive functional data for any purified Ipa protein. Here, we describe the first characterization of highly purified recombinant IpaC, which elicits numerous epithelial cell responses related to events that take place during pathogen invasion. 125I-labeled IpaC binds cultured Henle 407 intestinal cells with an apparent dissociation constant in the low micromolar range. Moreover, incubation of epithelial cells with IpaC results in general changes in cellular phosphoprotein content, demonstrating this protein's ability to influence cellular protein kinase activities. These results contrast dramatically with those seen for recombinant IpaD, which does not bind to or induce detectable changes in the normal activities of cultured epithelial cells. In addition to influencing host cell activities, preincubation of epithelial cells with purified IpaC enhances uptake of S. flexneri by host cells. A similar result is seen when the cells are preincubated with a highly concentrated water extract of virulent S. flexneri 2a (strain 2457T). Interestingly, soluble IpaC also appears to promote uptake of the noninvasive S. flexneri 2a strain BS103. Purified IpaD failed to enhance the uptake of virulent S. flexneri and did not facilitate uptake of BS103. Taken together, the data suggest that IpaC is a potential effector of the host cell biological activities and may be responsible for entry of S. flexneri into target cells.

Antigens, Bacterial↗

PubMed2003

The insecticidal toxin makes caterpillars floppy 2 (Mcf2) shows similarity to HrmA, an avirulence protein from a plant pathogen.

The Photorhabdus luminescens W14 toxin encoding gene makes caterpillars floppy (mcf) was discovered due to its ability to kill caterpillars when expressed in Escherichia coli. Here we describe a homologue of mcf (renamed as mcf1), termed mcf2, discovered in the same genome. The mcf2 gene predicts another large toxin whose central domain, like Mcf1, also shows limited homology to Clostridium cytotoxin B. However, the N-terminus of Mcf2 shows significant similarity to the type-III secreted effector HrmA from the plant pathogen Pseudomonas syringae and no similarity to the N-terminus of Mcf1. HrmA is a plant avirulence gene whose transient expression in tobacco cells results in cell death. Here we show that E. coli expressing Mcf2 can, like E. coli expressing Mcf1, kill insects. Further, expression of the c-Myc tagged N-terminus of Mcf2, the region showing similarity to HrmA, results in nuclear localisation of the fusion protein and subsequent destruction of transfected mammalian cells. The Mcf1 and Mcf2 toxins therefore belong to a family of high molecular mass toxins, differing at their N-termini, which encode different effector domains.

Amino Acid Sequence↗

PubMed2003

Innate immunity: sensing the environment and regulating the regulators.

PURPOSE OF REVIEW: Innate immune cells act as sensors for environmental pathogens and key regulators of pathogen-specific T-cell effector responses. The expression of Toll-like receptors is essential for these functions. Innate immunity is a rapidly evolving field. Great progress has been made in the past year in characterizing the signaling pathways downstream of Toll-like receptors, and the role of Toll-like receptors in the regulation of pathogen responses. RECENT FINDINGS: The ability to control the activation of regulatory T cells has emerged as a key function of innate immunity. Regulatory T cells are involved in the induction of tolerance and the prevention of harmful immune pathology, particularly T-cell responses directed against self-antigens. Toll-like receptor-mediated interactions between pathogen-stimulated innate immune cells and regulatory T cells result in the release of suppression by regulatory T cells, thus allowing pathogen-specific responses. However, pathogenic microorganisms may exploit this interaction to evade the host's response. In addition, recent studies raise the possibility that regulatory T cells may express some Toll-like receptor family members, thereby responding directly to pathogens. SUMMARY: A deeper understanding of the complex role of innate immune cells as sensors of the environment and regulators of pathogen responses will probably influence the current models of immune regulation, particularly those centered on the role of the environment in shaping immune responses.

CD4-Positive T-Lymphocytes↗

PubMed2003

Ectopic expression of Ralstonia solanacearum effector protein PopA early in invasion results in loss of virulence.

Ralstonia solanacearum OE1-1 (OE1-1) is pathogenic to tobacco. The type III-secreted effector protein popA of OE1-1 showed 97.6% identity to popA of R. solanacearum GMI1000, which is not pathogenic to tobacco. Reverse transcription-polymerase chain reaction analysis showed that popA in OE1-1 was expressed at 3 h after inoculation (HAI), but not before, in infiltrated-tobacco leaves. Pathogenicity analysis using a popABC operon-deleted mutant of OE1-1 (deltaABC) showed that popABC is not directly involved in the pathogenicity of OE1-1. When Papa, which constitutively expresses popA, was infiltrated into tobacco leaves, popA was expressed by 0.5 HAI. Papa could no longer multiply or spread in tobacco leaves and was no longer virulent. Moreover, the hypersensitive response (HR) and expression of HR-related genes were not induced in Papa-infiltrated leaves. Papa was also avirulent in a tobacco root-dipping inoculation assay. These results suggest that the expression of popA in Papa immediately after invasion triggers the suppression of bacterial proliferation and movement, resulting in loss of virulence. However, Papa retained its virulence when directly inoculated into xylem vessels. This result suggests that tobacco plants can recognize PopA when it is expressed early in disease development, and respond with an effective defense in the intercellular spaces.

Bacterial Proteins↗

PubMed2005

The hrpK operon of Pseudomonas syringae pv. tomato DC3000 encodes two proteins secreted by the type III (Hrp) protein secretion system: HopB1 and HrpK, a putative type III translocator.

Pseudomonas syringae is a gram-negative bacterial plant pathogen that is dependent on a type III protein secretion system (TTSS) and the effector proteins it translocates into plant cells for pathogenicity. The P. syringae TTSS is encoded by hrp-hrc genes that reside in a central region of a pathogenicity island (Pai). Flanking one side of this Pai is the exchangeable effector locus (EEL). We characterized the transcriptional expression of the open reading frames (ORFs) within the EEL of P. syringae pv. tomato DC3000. One of these ORFs, PSPTO1406 (hopB1) is expressed in the same transcriptional unit as hrpK. Both HopB1 and HrpK were secreted in culture and translocated into plant cells via the TTSS. However, the translocation of HrpK required its C-terminal half. HrpK shares low similarity with a putative translocator, HrpF, from Xanthomonas campestris pv. vesicatoria. DC3000 mutants lacking HrpK were significantly reduced in disease symptoms and multiplication in planta, whereas DC3000 hopB1 mutants produced phenotypes similar to the wild type. Additionally, hrpK mutants were reduced in their ability to elicit the hypersensitive response (HR), a programmed cell death associated with plant defense. The reduced HR phenotype exhibited by hrpK mutants was complemented by hrpK expressed in bacteria but not by HrpK transgenically expressed in tobacco, suggesting that HrpK does not function inside plant cells. Further experiments identified a C-terminal transmembrane domain within HrpK that is required for HrpK translocation. Taken together, HopB1 is a type III effector and HrpK plays an important role in the TTSS and is a putative type III translocator.

Amino Acid Sequence↗

PubMed2006

Identification and characterization of NleI, a new non-LEE-encoded effector of enteropathogenic Escherichia coli (EPEC).

Enteropathogenic Escherichia coli (EPEC), a major gastrointestinal pathogen, causes infantile diarrhea in many developing countries. EPEC is an attaching and effacing (A/E) pathogen that utilizes a LEE-encoded type III secretion system (TTSS) to deliver effector proteins into host cells. These effectors have been identified as potential virulence factors in A/E pathogens including EPEC, enterohemorrhagic E. coli (EHEC) and Citrobacter rodentium (CR). We used a proteomics approach to identify a new non-LEE-encoded effector, NleI, from the EPEC sepL and sepD mutants. The nleI gene, located in a prophage-associated island with nleBCD, is also present in EHEC and CR but not in E. coli K-12. In EPEC, the transcription of nleI was increased upon sepD inactivation but remained unaffected in ler and sepL mutants. We demonstrated that NleI is secreted and translocated into HeLa cells in a TTSS-dependent manner and that the CesT chaperone is required for efficient NleI translocation. Nevertheless, under overexpression conditions, the first 20 amino acids of NleI are sufficient to support both secretion and translocation. After translocation, NleI can be detected in the cytoplasmic and membrane of HeLa cells.

Blotting, Western↗

PubMed2000

Prevalence and polymorphism of genes encoding translocated effector proteins among clinical isolates of Salmonella enterica.

Pathogenic Salmonella enterica strains are capable of causing local and/or systemic infections. They employ two type III secretion systems to translocate an array of virulence-associated proteins (effector proteins) directly into the cytosol of target cells of the host. Earlier data had shown that changes in the repertoire of translocated effector proteins may contribute to the adaptation of Salmonella strains to new hosts and to the emergence of epidemic strains. Using PCR and Southern blot techniques the presence of and the polymorphism among the genes encoding the translocated effector proteins SopB, SopD, SopE, SopE2, SipA, SipB, SipC, AvrA, and SptP was studied in 71 phylogenetically well characterised S. enterica subspecies I (subspecies enterica) strains of the SARB collection and in 209 clinical and epidemic isolates of S. enterica subspecies I belonging to various serovars, phage types, and genotypes. All these Salmonella strains harbour all these respective genes with the exception of sopE and avrA which have been identified in only some of them. Several of the studied genes display genetic polymorphisms (RFLP). These RFLP patterns did not show a strict correlation with the genetic distance, the grouping genes in order to understand their role in the evolution of Salmonella as a pathogen.

Actins↗

PubMed2005

Virulence-associated type IV secretion systems of Bartonella.

Type IV secretion systems (T4SSs) are transport machineries of Gram-negative bacteria that mediate interbacterial DNA-transfer, and secretion of virulence factors into eukaryotic target cells. A growing number of human pathogenic bacteria use T4SSs for intercellular delivery of effector molecules that modify host cellular functions in favour of the pathogen. Recent advances in studying the molecular mechanisms of Bartonella pathogenesis have provided evidence for the central roles of two distinct T4SSs, VirB/VirD4 and Trw, in the ability of the bacteria to colonize, invade and persist within either vascular endothelial cells or erythrocytes, respectively. The identification of VirB/VirD4-transported substrates and the delineation of their secretion signal have paved the way towards understanding the molecular mechanisms underlying Bartonella-host cell interaction and modulation, as well as the exploitation of this system for engineered substrate delivery into mammalian target cells.

Bacterial Proteins↗