Disease relevance of ymt

• The Shiga toxigenic Escherichia coli (STEC) O113:H21 strain 98NK2, which was responsible for an outbreak of hemolytic uremic syndrome, secretes a highly potent and lethal subtilase cytotoxin that is unrelated to any bacterial toxin described to date [1].
• Oral immunization against cholera toxin with a live Yersinia enterocolitica carrier in mice [2].
• The genome of the TT01 strain of Photorhabdus luminescens was recently sequenced and a large number of toxin-encoding genes were found [3].
• Three novel tRNA genes present in the phage genome may serve to increase the availability of rare tRNA species associated with efficient expression of pathogenicity determinants: both the Shiga toxin and serine/threonine kinase genes contain rare isoleucine and arginine codons [4].
• The N-terminal peptide was found to show no inhibition of the proliferation induced by the other superantigen (staphylococcal enterotoxin B) or the other T-cell mitogen pertussis toxin, indicating that the inhibition is specific to YPM-induced proliferation [5].

High impact information on ymt

• All strains adhered in a localized pattern to, and induced actin aggregation in, HeLa cells, and produced a toxin that was lethal to Vero cells [6].
• Recombinant Y. enterocolitica strains expressing the B subunit of the cholera toxin were constructed from a yopH-ctxB operon fusion [2].
• Oral inoculation of recombinant bacteria in mice elicited serum and intestinal antibody responses and resulted in protection of the immunized mice against a cholera toxin challenge [2].
• The toxin causes alteration of the host cell actin cytoskeleton and promotes bacterial invasion of blood-brain barrier endothelial cells [7].
• Continuous exposure of mice to superantigenic toxins induces a high-level protracted expansion and an immunological memory in the toxin-reactive CD4+ T cells [8].

Chemical compound and disease context of ymt

• The RfaH protein controls the transcription of a specialized group of Escherichia coli and Salmonella operons that direct the synthesis, assembly and export of the lipopolysaccharide core, exopolysaccharide, F conjugation pilus and haemolysin toxin [9].
• The bacterial toxin Yersinia outer protein T (YopT) is a cysteine protease that cleaves Rho GTPases immediately upstream of a carboxyl-terminal isoprenylcysteine [10].
• Shiga toxin-producing E. coli O157 strains usually do not ferment sorbitol and are GUD-negative [11].
• Development of digoxigenin-labeled PCR amplicon probes for use in the detection and identification of enteropathogenic Yersinia and Shiga toxin-producing Escherichia coli from foods [12].

Biological context of ymt

• Through the search for genes upregulated at low growth temperatures in Yersinia enterocolitica strain W22703, a genomic island of 19 kb termed tc-PAI(Ye) with homologues of the toxin genes tcaA, tcaB, tcaC and tccC was identified [13].
• Our data show that the superantigenic toxin YPMa contributes to the virulence of Y. pseudotuberculosis in systemic infection in mice [14].
• The C-terminal 30 amino acids of the predicted protein exactly correspond to the amino acid sequence of the toxin extracted from culture supernatants (T. Takao, N. Tominaga, and Y. Shimonishi, Biochem. Biophys. Res. Commun. 125:845-851, 1984) [15].
• These data indicate that YopJ functions as a "MAP kinase toxin" to selectively block nuclear responses that are triggered by Yersinia-host cell interaction [16].
• On the basis of the published nucleotide sequences of the genes that code for the heat-labile toxin LTh and the heat-stable toxins STaI and STaII of human enterotoxigenic Escherichia coli, a 34-mer and two 33-mer oligonucleotide probes were synthesized [17].

Anatomical context of ymt

• LcrV, a substrate for Yersinia enterocolitica type III secretion, is required for toxin targeting into the cytosol of HeLa cells [18].
• Diagnostic tests were complete blood cell count; electrolytes; stool for occult blood, white blood cells, and Clostridia difficile toxin; and stool culture for Shigella, Salmonella, Yersinia, and Campylobacter [19].
• Subtle events at, or within, the cell membrane must occur during intoxication and may include complex associations of toxin with membrane lipid and protein components [20].
• Cyclic adenosine 3',5'-monophosphate levels in both intestines and cultured cells were not affected by the toxin [21].
• In analogy with Vibrio cholerae and other toxigenic enteropathogens such as Yersinia enterocolitica it seems most likely today that H. pylori by specific surface proteins binds to epithelial cell receptors (Table 1) allowing the pathogen to deliver urease, vacuolating toxin and other toxic metabolites to cause tissue damage and inflammation (1-3) [22].

Associations of ymt with chemical compounds

• The toxin produced by this noninvasive (serogroup O6) strain resembled YST in terms of molecular size, heat stability, and solubility in methanol [23].
• Measurement of antibacterial activities of T-2 toxin, deoxynivalenol, ochratoxin A, aflatoxin B1 and fumonisin B1 using microtitration tray-based turbidimetric techniques [24].
• T-2 toxin, deoxynivalenol (DON), ochratoxin A (OTA), aflatoxin B1 (AFB1) and fumonisin B1 (FB1) were used as representative mycotoxins [24].
• The data obtained indicate that bacterial growth can be inhibited especially by T-2 toxin, aflatoxin B1 and ochratoxin A and that this effect can be partially counteracted by antioxidants such as coenzyme Q10 plus l-carnitine [25].

Analytical, diagnostic and therapeutic context of ymt

• Shiga toxin-producing (STEC), attaching-and-effacing (A/EEC), enteropathogenic (EPEC), enterotoxigenic, enteroinvasive, and enteroaggregative Escherichia coli were detected by using colony hybridization with virulence gene probes and serotyping [26].
• This purified protein showed cross-reactivity to the binding subunit of cholera toxin in western immunoblot [27].
• Humoral immunity to plague was improved further, resulting in 80% protection from challenge, if a relatively high dose (10 micrograms) of cholera toxin B subunit was added to the microsphere suspension prior to intra-nasal delivery [28].
• We conclude that in this animal model of pneumonic plague, intra-nasal administration of microgram quantities of Yersinia pestis subunits confers protective immunity, provided the vaccines are microencapsulated or admixed with a strong mucosal adjuvant, such as the cholera toxin B subunit [28].
• Extending this work to toxin-antitoxin relationships, Martin provided evidence that antitoxin was a large molecule with slow diffusibility in tissue and advised the administration of curative serum (including diphtheria antitoxin) by intravenous injection [29].

References