Disease relevance of Yersinia

• A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis [1].
• NE also preferentially cleaves virulence factors of Salmonella and Yersinia [2].
• In situ production of interleukin 1 alpha (IL-1 alpha) and IL-1 beta was investigated in Peyer's patches (PP) of mice undergoing an acute bacterial infection with Yersinia enterocolitica O8 [3].
• We report a case of spontaneous Yersinia enterocolitica peritonitis revealing idiopathic hemochromatosis in a 62-yr-old man with fever and diarrhea [4].
• In complement-fixation assays, the sera from the Crohn's disease patients had enhanced reactivity compared with the control sera to all seven orally ingested pathogens studied; however, only the difference in distribution of titers to Yersinia pseudotuberculosis was statistically significant (p less than 0.0025) [5].

Psychiatry related information on Yersinia

• OBJECTIVE: To dissect the host defense mechanisms in relation to the development of Yersinia-associated arthritis by evaluating the impact of tumor necrosis factor receptor p55 (TNFRp55) deficiency on Yersinia enterocolitica infection [6].
• This life style requires a sophisticated anti-host strategy, which is implemented by the Yersinia virulence plasmid [7].

High impact information on Yersinia

• Bacterial strains harboring the Yersinia pseudotuberculosis inv locus were analyzed in order to investigate the mechanism of host cell penetration by an invasive pathogen [8].
• Yersinia lead SUMO attack [9].
• Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate [10].
• Increased virulence of Yersinia pseudotuberculosis by two independent mutations [11].
• Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector [12].

Chemical compound and disease context of Yersinia

• Amino acids surrounding an essential Cys residue are highly conserved, as are other amino acids in the Yersinia and mammalian protein tyrosine phosphatases, suggesting that they use a common catalytic mechanism [13].
• Controlled trial of tetracycline prophylaxis in individuals with persistently raised Yersinia enterocolitica antibody titres [14].
• METHODS: Proximal colon from rabbits infected with Yersinia entercolitica, a pair-fed group, and controls was mounted in Ussing chambers, and Na+ transport, short-circuit current, and tissue conductance were examined during a basal period and after stimulation with the SCFAs, butyrate, or propionate [15].
• This fragment, which is necessary and sufficient for Tir interaction, defines a new super domain in intimin that exhibits striking structural similarity to the integrin-binding domain of the Yersinia invasin and C-type lectin families [16].
• Yersiniabactin (Ybt) synthetase is a three-subunit, 17-domain [7 domains in high molecular weight protein (HMWP)2, 9 in HMWP1, and 1 in YbtE] enzyme producing the virulence-conferring siderophore yersiniabactin in Yersinia pestis [17].

Biological context of Yersinia

• Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia [13].
• The 70-kb virulence plasmid enables Yersinia spp [18].
• RESULTS: H. pylori induced phosphorylation of 125-130-kilodalton proteins, similar in size to the target proteins of Yersinia YopH [19].
• Additional pagP homologs are encoded in the genomes of YERSINIA: and BORDETELLA: species [20].
• The predicted amino acid sequence derived from the nucleotide sequence of eae shows significant homology to that of the invasin of Yersinia pseudotuberculosis [21].

Anatomical context of Yersinia

• In this study, we investigated the activity of transcription factor NF-kappaB in macrophages infected with Yersinia enterocolitica [22].
• The adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activation [23].
• We infected the murine macrophage-like cell line J774A.1 with Yersinia pseudotuberculosis and investigated the specificity of YopH and YopHC403A, a catalytically inactive mutant derivative, for eukaryotic phosphoproteins [24].
• These findings were verified in murine peritoneal macrophages by using recombinant LcrV truncates representing aa 1-130 from different Yersinia spp [25].
• The activation response of neutrophils to nonpathogenic bacteria is greatly altered by exposure to Yersinia pestis, which may be a major factor contributing to the virulence and rapid progression of plague [26].

Gene context of Yersinia

• The increased resistance in casp-1(-/)- animals appears specific for Salmonella infection since these mice were susceptible to colonization by another enteric pathogen, Yersinia pseudotuberculosis, which normally invades the PP [27].
• The impact of this immunosuppressive effect for yersinia pathogenesis is underlined by the observation that TLR2-deficient mice are less susceptible to oral Y. enterocolitica infection than isogenic wild-type animals [28].
• TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors [29].
• Sequencing of codons 25-92 of the lcrV gene from 59 strains of the three pathogenic Yersinia species revealed a hypervariable hotspot within aa 40-61 [25].
• A hypervariable N-terminal region of Yersinia LcrV determines Toll-like receptor 2-mediated IL-10 induction and mouse virulence [25].

Analytical, diagnostic and therapeutic context of Yersinia

• Site-directed mutagenesis, combined with detailed kinetic and mechanistic studies of Yersinia PTP, have contributed greatly to the understanding of the chemical mechanism for PTP catalysis, the nature of the enzymatic transition state, and the means by which the transition state is stabilized [30].
• Identification of these crossreactive envelope proteins was achieved by Western blotting using affinity-purified anti-Y. enterocolitica antibodies that specifically react with the TSHR and, conversely, for envelope proteins of Yersinia [31].
• Molecular cloning, iron-regulation and mutagenesis of the irp2 gene encoding HMWP2, a protein specific for the highly pathogenic Yersinia [32].
• By immunoblotting using rabbit antibodies against Irp65 and chrome azurol S-agar, we were able to demonstrate that all tested mouse-lethal Y. enterocolitica and Yersinia pseudotuberculosis strains of different serotypes express siderophores and Irp65 [33].
• CopN is homologous to the secreted protein YopN of Yersinia sp., and analysis of monolayers 20 h after infection via indirect immunofluorescence showed specific labelling of inclusion membranes when probed with CopN-specific antibodies but not with Scc1-specific antibodies [34].

References