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Shiga ToxinShiga Toxin 2Shiga Toxin 1Shiga ToxinsShigella dysenteriaeShiga-Toxigenic Escherichia coliEscherichia coli O157Hemolytic-Uremic SyndromeEscherichia coli InfectionsEnterohemorrhagic Escherichia coliBacterial ToxinsMolecular Sequence DataCholera ToxinProtein SubunitsEscherichia coliAmino Acid SequenceCatalytic DomainCytotoxinsT-2 ToxinTrihexosylceramidesRicinGlobosidesMacromolecular SubstancesProphagesProtein Phosphatase 2DNA-Activated Protein KinasePhosphoprotein PhosphatasesBase SequenceVero CellsEscherichia coli ProteinsRibosome Inactivating ProteinsTetanus ToxinAntitoxinsCyclic AMP-Dependent Protein KinasesProtein BindingProtein KinasesCattleFecesCell LineKineticsCercopithecus aethiopsBinding SitesAdhesins, BacterialProtein Phosphatase 1MutationVirulence FactorsDiarrheaHeLa CellsPhosphorylationCatalysisSerotypingBotulinum Toxins, Type AEscherichia coli VaccinesMarine ToxinsTelomeraseDysentery, BacillaryVirulenceRecombinant ProteinsEnterotoxinsPolymerase Chain ReactionCloning, MolecularRabbitsCyclic AMPShigellaBacteriophagesSequence Homology, Amino AcidButyric AcidEnzyme ActivationProtein ConformationToxoidsDNA-Binding ProteinsRecombinant Fusion ProteinsHemolysin ProteinsCells, CulturedModels, MolecularMolecular WeightEdema Disease of SwineColiphagesRNA, MessengerGlutamate-Cysteine LigaseElectrophoresis, Polyacrylamide GelMutagenesis, Site-DirectedGolgi ApparatusProtein-Serine-Threonine KinasesGenes, BacterialDNA, BacterialAntibodies, BacterialProtein Structure, TertiaryPeptide FragmentsCarrier ProteinsSaccharomyces cerevisiaeDNA PrimersProtein TransportCattle DiseasesPlasmidsCyclic AMP-Dependent Protein Kinase Catalytic SubunitsRNA, Ribosomal, 28SFood MicrobiologyGlycolipidsSignal Transduction

ProteinsMembranesFacilitatesProteinDomainCholera toxinEscherichiaBacterialEukaryoticRibosomalBindsHemolyticExotoxinColiRibosomesProteolyticallySTECPertussisMammalianResiduesVirulenceStructuralDissociationTargetsBordetellaSubsetMechanismLipidCytosolIntestinalInactivationConsistsInducesMembraneSimilarActivityLargeSpecificActivePreparation

Proteins2

• Members of the family include shiga toxins, and type I (e.g. trichosanthin and luffin) and type II (e.g. ricin, agglutinin, and abrin) ribosome inactivating proteins (RIPs). (wikipedia.org)
• The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. (bvsalud.org)

Membranes1

• Bacillus thuringiensis toxin Cyt2Aa forms filamentous oligomers when exposed to lipid membranes or detergents. (ki.si)

Facilitates1

• The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. (bvsalud.org)

Protein1

• Examples include: Abrin Beetin Ricin Saporin Shiga toxin A Spiroplasma toxin Trichosanthin Viscumin (European mistletoe) Pokeweed antiviral protein (Phytolacca americana) Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD (October 1993). (wikipedia.org)

Domain1

• Type II (AB): RIPs-II are composed of an A domain with similar catalytic activity to Type I RIPs, and a B domain with carbohydrate-binding (lectin) properties. (wikipedia.org)

Cholera toxin10

• AB toxins include Shiga toxin (ST) from Escherichia coli strains such as O157:H7, cholera toxin (CT) from Vibrio cholerae, heat-labile toxin (LT) from enterotoxigenic E. coli, diphtheria toxin (DT) from Corynebacterium diphtheriae, exotoxin A (ETA) from Pseudomonas aeruginosa, and ricin from the plant Ricinus communis. (usda.gov)
• Despite its heterogeneous subunit composition, the structure of the cell-binding B-oligomer (S2, S3, two copies of S4, and S5) resembles the symmetrical B-pentamers of the cholera toxin and Shiga toxin families, but it interacts differently with the A-subunit. (nih.gov)
• Enterotoxins (cholera toxin [CT] or STb), which selectively upregulate fluid secretion are the most potent diarrheagenic toxins. (medscape.com)
• Other members of the cholera toxin family are the E. coli heat-labile enterotoxins (LT)-I and-II. (medscape.com)
• Cholera toxin, via the B-subunits, binds with high affinity to GM1 ganglioside, which is distributed in the detergent-resistant membrane fraction of enterocytes. (medscape.com)
• The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. (nih.gov)
• The nontoxic, pentameric B protomer of cholera toxin. (nih.gov)
• The cell membrane binding component of cholera toxin. (nih.gov)
• Detoxified aggregate of cholera toxin formed by heat treatment of purified cholera toxin. (nih.gov)
• The catalytic subunit of cholera toxin. (nih.gov)

Escherichia6

• Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. (wikipedia.org)
• Subtilase cytotoxin (SubAB) is the prototype of a recently discovered AB(5) cytotoxin family produced by certain strains of Shiga toxigenic Escherichia coli (STEC). (nih.gov)
• A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli. (nih.gov)
• Background: Shiga toxin-producing Escherichia coli (STEC) are a subset of pathogens leading to illnesses such as diarrhea, hemolytic uremic syndrome and even death. (diamond.ac.uk)
• the carboxy-terminal domain of the transcription factor escherichia coli nusa, nusactd, interacts with the protein n of bacteriophage lambda, lambdan, and the carboxyl terminus of the e. coli rna polymerase alpha subunit, alphactd. (liverpool.ac.uk)
• Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. (lookformedical.com)

Bacterial7

• Several plant and bacterial toxins, the AB toxins, share a common structural organization that consists of a catalytic A subunit and a cell-binding B subunit. (usda.gov)
• This group excludes bacterial AB5 toxins such as Shiga toxin, as the carbohydrate-binding ability evolved separately and these toxins are more similar to type I RIPs. (wikipedia.org)
• The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism. (nih.gov)
• The structure provides insight into the pathogenic mechanisms of pertussis toxin and the evolution of bacterial toxins. (nih.gov)
• Many bacterial toxins have the ability to enter target cells, most often by using physiological endocytosis pathways, and to modify a specific intracellular target ( Table 3 ). (medscape.com)
• CT and LT subunits are exported across the bacterial membrane by the type II secretion pathways, and assemble in the periplasm. (medscape.com)
• The bacterial 70S ribosome is composed of a 50S large subunit and a 30S small subunit. (lookformedical.com)

Eukaryotic3

• These toxins are released into the extracellular milieu, but they act upon targets within the eukaryotic (mammalian) cytosol. (usda.gov)
• Two peripheral domains that are unique to the pertussis toxin B-oligomer show unexpected structural homology with a calcium-dependent eukaryotic lectin, and reveal possible receptor-binding sites. (nih.gov)
• The eukaryotic 80S ribosome is composed of a 60S large subunit and a 40S small subunit. (lookformedical.com)

Ribosomal4

• They inactivate 60S ribosomal subunits by an N-glycosidic cleavage, which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA. (wikipedia.org)
• Cryo-EM structure of Shiga toxin 2 in complex with the native ribosomal P-stalk reveals residues involved in the binding interaction. (nih.gov)
• They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. (lookformedical.com)
• The two dissimilar sized ribonucleoprotein complexes that comprise a RIBOSOME - the large ribosomal subunit and the small ribosomal subunit. (lookformedical.com)

Binds1

• In the intoxication process, the Hly portion of the toxin binds to CR3 receptor on target cells (CD11b + ) and allows translocation of the AC enzyme into the cell. (listlabs.com)

Hemolytic1

• Here, we show that intraperitoneal injection of SubAB causes microangiopathic hemolytic anemia, thrombocytopenia, and renal impairment in mice--characteristics typical of Shiga toxin-induced hemolytic uremic syndrome. (nih.gov)

Exotoxin1

• Pertussis toxin is an exotoxin of the A-B class produced by Bordetella pertussis. (nih.gov)

Coli1

• Four enzymatic DNA library preparation kits were compared for sequencing Shiga toxin-producing E. coli. (worldcarecouncil.org)

Ribosomes1

• The small subunit of eubacterial RIBOSOMES. (lookformedical.com)

Proteolytically2

• The A-subunit is proteolytically activated by a V. cholerae endopeptidase into two components A1 (22 kDa) and A2 (5.5 kDa), which remain linked by a disulfide bridge. (medscape.com)
• The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. (nih.gov)

STEC1

• These findings raise the possibility that SubAB directly contributes to pathology in humans infected with strains of STEC that produce both Shiga toxin and SubAB. (nih.gov)

Pertussis8

• The crystal structure of pertussis toxin has been determined at 2.9 A resolution. (nih.gov)
• Adenylate cyclase toxin-hemolysin (ACT, AC-Hly, or CyaA) is an important virulence factor for Bordetella pertussis . (listlabs.com)
• Although the catalytic activity in this AC toxoid is destroyed, it is still cell invasive and able to induce an immune response to co-administered pertussis antigens (10 , 11, 12) . (listlabs.com)
• List Labs provides several variations of the B. pertussis Adenylate Cyclase Toxin. (listlabs.com)
• Sebo P., Osicka R., Masin J., (2014) Adenylate cyclase toxin-hemolysin relevance for pertussis vaccines. (listlabs.com)
• 1994) Adenylate cyclase toxin from Bordetella pertussis produces ion conductance across artificial lipid bilayers in a calcium and polarity-dependent manner. (listlabs.com)
• Simsova M., Sebo P., Leclerc C., (2004) The adenylate cyclase toxin from Bordetella pertussis-a novel promising vehicle for antigen delivery to dendritic cells. (listlabs.com)
• Macdonald-Fyall J., Xing D., Corbel M., Baillie S., Parton R., Coote J., (2004) Adjuvanticity of native and detoxified adenylate cyclase toxin of Bordetella pertussis towards co-administered antigens. (listlabs.com)

Mammalian1

• To reach their targets in the cytosol of mammalian cells the toxins apparently go one step further and cross the ER membrane. (rupress.org)

Residues2

• The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). (nih.gov)
• Adenylate cyclase toxin is a large (178 kDa), 1,706-residue-long, toxin consisting of an amino-terminal adenylate cyclase (AC) domain of 400 residues and a repeat toxin (RTX) moiety of 1,306 residues. (listlabs.com)

Virulence1

• The Shiga toxins are the main virulence factors and divided in two groups: Stx1 and Stx2, of which the latter is more frequently associated with severe pathologies in humans. (diamond.ac.uk)

Structural1

• The structural similarity is all the more surprising given that there is almost no sequence homology between B-subunits of the different toxins. (nih.gov)

Dissociation2

• Yet the extract did not affect toxin transport from the cell surface to the ER or the dissociation of CTA1 from its holotoxin. (usda.gov)
• Dissociation of the A-subunits from the B-pentamer in the Golgi or ER is still under discussion. (medscape.com)

Targets2

• Despite the general similarities in their host interactions, each AB toxin utilizes a distinct subset of surface receptors, intracellular trafficking/translocation mechanisms and cytosolic targets. (usda.gov)
• Adenylate cyclase toxin targets sentinel cells of the host's innate immune defense. (listlabs.com)

Bordetella1

• Vojtova J., Kamanova J., Sebo P., (2006) Bordetella adenylate cyclase toxin: a swift saboteur of host defense. (listlabs.com)

Subset1

• A specific subset of host-toxin interactions were thus disrupted by the application of grape extract, as opposed to a gross alteration of toxin or cellular function. (usda.gov)

Mechanism2

• Other AB toxins such as ST and CT move from the plasma membrane to the endoplasmic reticulum (ER) before passage into the cytosol through a mechanism involving the quality control system of ER-associated degradation (ERAD). (usda.gov)
• However, B-subunits lacking an ER retention signal or CT mutated on the KDEL motif are also transported to the ER, via an unknown mechanism. (medscape.com)

Lipid1

• GM1 directs the toxin into lipid rafts, which facilitates toxin entry into noncoated vesicles, but also into clathrin-coated vesicles. (medscape.com)

Cytosol2

• Some AB toxins, such as DT, access the cytosol from acidified endosomes. (usda.gov)
• and (vi) translocation of the A subunit through a membrane-spanning pore into the cytosol. (usda.gov)

Intestinal2

• Intracellularly active toxins usually display a unique enzymatic activity, but they can stimulate several cell signaling pathways, which often results in intestinal cell necrosis, leading to a mid-to-severe inflammatory response. (medscape.com)
• The inflammatory process, which can also be triggered by other toxin-induced cell signaling, contributes to the damage of the intestinal mucosa. (medscape.com)

Inactivation1

• It is therefore difficult to inhibit multiple AB toxins with a single agent for inactivation. (usda.gov)

Consists1

• It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. (nih.gov)

Induces1

• The toxin is lethal for mice, but the pathology it induces is poorly understood. (nih.gov)

Membrane2

• The toxins must therefore cross a membrane barrier in order to function. (usda.gov)
• BACKGROUND: The resistance of a Culex quinquefasciatus strain to the binary (Bin) larvicidal toxin from Lysinibacillus sphaericus is due to the lack of expression of the toxin's receptors, the membrane-bound Cqm1 α-glucosidases. (bvsalud.org)

Similar2

• Type II (AB): RIPs-II are composed of an A domain with similar catalytic activity to Type I RIPs, and a B domain with carbohydrate-binding (lectin) properties. (wikipedia.org)
• Similar to Shiga toxin (Stx), CT and LTs consist of an A-subunit (28 kDa), and five B-subunits (11 kDa each) assembled in a pentamer (AB5 structure). (medscape.com)

Activity1

• and (iv) inhibiting the catalytic activity of CTA1. (usda.gov)

Large4

• Toxin-antitoxin (TA) systems are a large group of small genetic modules found in prokaryotes and their mobile genetic elements. (bvsalud.org)
• Using our tool NetFlax (standing for Network-FlaGs for toxins and antitoxins), we have performed a large-scale bioinformatic analysis of proteinaceous TAs, revealing interconnected clusters constituting a core network of TA-like gene pairs. (bvsalud.org)
• The large subunit of the eubacterial 70s ribosome. (lookformedical.com)
• The large subunit of the 80s ribosome of eukaryotes. (lookformedical.com)

Specific1

• The catalytic A subunit is a highly specific subtilase-like serine protease that cleaves the endoplasmic reticulum chaperone BiP. (nih.gov)

Active1

• Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I". Proceedings of the National Academy of Sciences of the United States of America. (wikipedia.org)

Preparation1

• Additionally we have samples available of the Genetically Detoxified CyaA-AC Toxoid, request Product #188X, and samples of an especially low endotoxin preparation of Adenylate Cyclase Toxin Product #188U. (listlabs.com)