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Bacterial Effector Proteins (bacterial + effector_protein)
Selected AbstractsIdentification and characterization of NleA, a non-LEE-encoded type III translocated virulence factor of enterohaemorrhagic Escherichia coli O157:H7MOLECULAR MICROBIOLOGY, Issue 5 2004Samantha Gruenheid Summary Enterohaemorrhagic Escherichia coli (EHEC) O157:H7 uses a specialized protein translocation apparatus, the type III secretion system (TTSS), to deliver bacterial effector proteins into host cells. These effectors interfere with host cytoskeletal pathways and signalling cascades to facilitate bacterial survival and replication and promote disease. The genes encoding the TTSS and all known type III secreted effectors in EHEC are localized in a single pathogenicity island on the bacterial chromosome known as the locus for enterocyte effacement (LEE). In this study, we performed a proteomic analysis of proteins secreted by the LEE-encoded TTSS of EHEC. In addition to known LEE-encoded type III secreted proteins, such as EspA, EspB and Tir, a novel protein, NleA (non- LEE-encoded effector A), was identified. NleA is encoded in a prophage-associated pathogenicity island within the EHEC genome, distinct from the LEE. The LEE-encoded TTSS directs translocation of NleA into host cells, where it localizes to the Golgi apparatus. In a panel of strains examined by Southern blot and database analyses, nleA was found to be present in all other LEE-containing pathogens examined, including enteropathogenic E. coli and Citrobacter rodentium, and was absent from non-pathogenic strains of E. coli and non-LEE-containing pathogens. NleA was determined to play a key role in virulence of C. rodentium in a mouse infection model. [source] IpgD, a protein secreted by the type III secretion machinery of Shigella flexneri, is chaperoned by IpgE and implicated in entry focus formationMOLECULAR MICROBIOLOGY, Issue 1 2000Kirsten Niebuhr Invasion of epithelial cells by Shigella flexneri involves entry and intercellular dissemination. Entry of bacteria into non-phagocytic cells requires the IpaA,D proteins that are secreted by the Mxi,Spa type III secretion machinery. Type III secretion systems are found in several Gram-negative pathogens and serve to inject bacterial effector proteins directly into the cytoplasm of host cells. In this study, we have analysed the IpgD protein of S. flexneri, the gene of which is located on the virulence plasmid at the 5, end of the mxi,spa locus. We have shown that IpgD (i) is stored in the bacterial cytoplasm in association with a specific chaperone, IpgE; (ii) is secreted by the Mxi,Spa type III secretion system in amounts similar to those of the IpaA,D proteins; (iii) is associated with IpaA in the extracellular medium; and (iv) is involved in the modulation of the host cell response after contact of the bacterium with epithelial cells. This suggests that IpgD is an effector that might be injected into host cells to manipulate cellular processes during infection. [source] Non-host resistance in plants: new insights into an old phenomenonMOLECULAR PLANT PATHOLOGY, Issue 3 2005THORSTEN NÜRNBERGER SUMMARY Resistance of an entire plant species to all isolates of a microbial species is referred to as non-host or species resistance. An interplay of both constitutive barriers and inducible reactions comprises the basis for this most durable form of plant disease resistance. Activation of inducible plant defence responses is probably brought about by the recognition of invariant pathogen-associated molecular patterns (PAMP) that are characteristic of whole classes of microbial organisms. PAMP perception systems and PAMP-induced signalling cascades partially resemble those known to mediate activation of innate immune responses in animals, suggesting an evolutionarily ancient molecular concept of non-self recognition and immunity in eukaryotes. Genetic dissection has recently provided clues for SNARE-complex-mediated exocytosis and directed vesicle trafficking in executing plant non-host resistance. Recent functional analysis of bacterial effector proteins indicates that establishment of infection in susceptible plants is associated with suppression of plant species resistance. [source] A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1CELLULAR MICROBIOLOGY, Issue 5 2006Andrea Haraga Summary Essential to salmonellae pathogenesis is an export device called the type III secretion system (TTSS), which mediates the transfer of bacterial effector proteins from the bacterial cell into the host cell cytoplasm. Once inside the host cell, these effectors are then capable of altering a variety of host cellular functions in order to promote bacterial survival and colonization. SspH1 is a Salmonella enterica serovar Typhimurium TTSS effector that localizes to the mammalian nucleus and down-modulates production of proinflammatory cytokines by inhibiting nuclear factor (NF)-,B-dependent gene expression. To identify mammalian binding partners of SspH1 a yeast two-hybrid screen against a human spleen cDNA library was performed. It yielded a serine/threonine protein kinase called protein kinase N 1 (PKN1). The leucine-rich repeat domain of SspH1 was demonstrated to mediate this interaction and also inhibition of NF-,B-dependent gene expression. This suggested that PKN1 may play a role in modulation of the NF-,B signalling pathway. Indeed, we found that expression of constitutively active PKN1 in mammalian cells results in a decrease, while depletion of PKN1 by RNA interference causes an increase in NF-,B-dependent reporter gene expression. These data indicate that SspH1 may inhibit the host's inflammatory response by interacting with PKN1. [source] Genome-wide analysis of host responses to the Pseudomonas aeruginosa type III secretion system yields synergistic effectsCELLULAR MICROBIOLOGY, Issue 11 2005Jeffrey K. Ichikawa Summary The type III secretion system (TTSS) is a dedicated bacterial pathogen protein targeting system that directly affects host cell signalling and response pathways. Our goal was to identify host responses to the Pseudomonas aeruginosa effectors, introduced into target cells utilizing the TTSS. We carried out expression profiling of a human lung pneumocyte cell line A549 exposed to isogenic mutants of P. aeruginosa PAK lacking individual or a combination of TTSS components. We then devised a data analysis method to isolate the key responses to specific secreted bacterial effector proteins as well as components of the TTSS machinery. Individually, the effector proteins elicited host responses consistent with their known functions, many of which were cell cycle-related. However, our analysis has shown that the effector proteins elicit a distinct host transcriptional response when present in combination, suggesting a synergistic effect. Furthermore, the pattern of host transcriptional responses is consistent with the pore forming ability of the TTSS needle complex. This study shows that the individual components of the TTSS define an integrated system and that a systems biology approach is required to fully understand the complex interplay between pathogen and host. [source] | ||||||||||