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US7427404B1 - Pertussis toxin mutants, bordetella strains

Therefore, cells + (+. ® ® ® ® ® ™ ™ ™ 1,. (() Targeted delivery of an ADP-ribosylating bacterial toxin into cancer cells. We incubated his-tagged yeast eEF2 (1.2 μg) with 2 μL biotinylated NAD+, 10 μL BSA (2 g/L), 10 μL l-arginine (100 mmol/L), 1 μL ADP-ribosylating compound [DT, PE, and cholera toxin (CT); all obtained from Sigma], chimeric toxins (DTA-EGF or scFv-PE; 10 to 1000 ng/L), and reaction buffer in a total volume of 100 μL at 37 °C for 2 h, transferred it into the precoated wells, and incubated ADP-RIBOSYLATING TOXINS.

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ExoA is a potent ADP-ribosylating toxin that spe- was digested with tobacco etch virus (1:10 ratio) at 4 °C. 2014-12-31 An ADP-ribosylating toxin from Listeria monocytogenes is disclosed, together with mutant toxins and uses therefor.There is only a low level of sequence identity between this toxin and known toxins such as the iota toxin from Clostridium perfringens. ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. Improper ADP-ribosylation has been implicated in some forms of cancer. It is also the basis for the toxicity of bacterial compounds such as cholera toxin, diphtheria toxin, and others. ADP-ribosylating toxins.

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CARDS TX secondary structure is indicated at the top. The R–STS/T–E signature motif is shared by CTxg members (yellow). two other ADP-ribosylating toxins, Escherichia coli heat-labile enterotoxin and cholera toxin.

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For the convenience of the reader, the various topics have been grouped into several sections: (a) poly(ADP-ribosyl)ation; (b) mono-ADP-ribosylation; (c) toxin  ADP-ribosylation is a ubiquitous post-translational addition of either monomers or by ADP-ribosyltransferases, usually by interferon-inducible diphtheria toxin-like Consequently, less is known about the antiviral effects of ADP-ribosylation. ADP-ribosylation is involved in the regulation of DNA repair, transcription, and other processes. The 18 human ADP-ribose transferases with diphtheria toxin  With only a single amino acid replacement cholera toxin CTA1 can be rendered while the native ADP-ribosylating molecule is a strong mucosal adjuvant. New pertussis toxin (PT) mutants are described being immunologically active and Chiron Corporation, Detoxified mutants of bacterial ADP-ribosylating toxins  Bakteriella toxiner — Vidare har C. Botulinum C3 ADP-ribosylater GTP-bindande proteiner Rho och Ras och Pertussis-toxin ADP-Ribosylates Gi  Chemical probes to study ADP-ribosylation: synthesis and biochemical as a potent but unselective inhibitor of diphtheria toxin-like ADP-ribosyltransferase 3  An ADP-ribosylating polypeptide produced by CORYNEBACTERIUM DIPHTHERIAE that causes the signs and symptoms of DIPHTHERIA. It can be broken into  ADP-ribosylating toxins and their endogenous relatives.

Passador L(1), Iglewski W. Author information: (1)Department of Microbiology and Immunology, University of Rochester, School of Medicine and Dentistry, New York 14642. PMID: 8057931 [Indexed for MEDLINE] Publication Types: Review; MeSH terms. ADP Ribose Transferases* Adenosine Diphosphate Ribose/metabolism* Bacterial Toxins/analysis ADP-ribosylating toxins have been the focus of intensive research for more than 30 years.
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Strikingly, the disruption of lipid rafts by cyclodextrin or membrane solubilization  The bacterial toxins and C3 enzyme have proven extremely useful in studies on signal transduction pathways in various cell types of eukaryotes. MonoADP-  Fig. 5: ADP- Ribosylation of a Target Host Protein by an A-B Toxin. The A component of most A-B toxins catalyzes ADP-ribosylation of host cell target proteins.

Second, the ADP-ribosylating toxins provide potent and often unique pharmacological tools for the study of the physiological functions of their target proteins. The latter is especially the case with cholera and pertussis toxins, which both modify the IX-subunits of heterotrimeric G-proteins involved in signal transduction pathways.
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ferases, which ADP-ribosylate Rho GTPases at Asn41 (6–8), and Pseudomonas aeruginosa exoenzyme S, which modifies Ras proteins at several arginine residues (9). Another member of the family of ADP-ribosylating toxins is the mosquitocidal toxin (MTX),1 which is produced by the low-toxicity strain SSII-1 of Bacillus sphaericus. The toxin is lethal The ADP-Ribosylating Toxin, AexT, from Aeromonas salmonicida subsp. salmonicida Is Translocated via a Type III Secretion Pathway Sarah E. Burr, Katja Stuber,† and Joachim Frey* Institute of Veterinary Bacteriology, University of Berne, CH-3012 Berne, Switzerland Received 14 February 2003/Accepted 26 August 2003 ADP-ribosyl transferase subunit of typhoid toxin from Salmonella typhi (exclusively human pathogen) is structurally similar to pertussis toxin; however, the pathogenic mechanisms as well as the proteins substrate(s) of this toxin remain unknown .

US7427404B1 - Pertussis toxin mutants, bordetella strains

B cells targeting. Sammanfattning: The ADP-ribosylating enterotoxins, cholera toxin  av S Deindl · 2019 — an early toxin in Pseudomonas infection.

two other ADP-ribosylating toxins, Escherichia coli heat-labile enterotoxin and cholera toxin. As noted earlier, virulence fac-tors, like classical bacterial toxins, have been heretofore unde-tected among pathogenic mycoplasmas. Site-Directed Mutagenesis, Expression, and Purification of Recombi-nant CARDS TX (rCARDS TX). Due to inherent slow growth and The observed pleiotropic effects are the result of the ability of S1 to ADP-ribosylate certain inhibitory α-subunits of heterotrimeric GTP-binding proteins (G-proteins) involved in a variety of signaling pathways. ADP-ribosylation of actin was also catalyzed by the 32 kDa C-terminal fragment of TccC3, which shows sequence similarity with ADP-ribosyltransferases, indicating a harboring of the enzyme activity . Actin is also ADP-ribosylated by the family of binary ADP-ribosylating toxins, including C2 toxin from C. botulinum and iota toxin from C. perfringens ( 9 ). MTX 30–870 is the native form of the ADP-ribosylating toxin from B. sphaericus SSII-1, which lacks the putative signal sequence of 29 amino acids. The toxin is reportedly proteolytically cleaved into a 27-kDa N-terminal fragment and a 70-kDa C-terminal fragment 1994-01-01 · Photoaffinity Labeling of Active Site Residues in ADP-Ribosylating Toxins By STEPHEN F. CARROLL and R. JOHN COLLIER Introduction The ADP-ribosylating toxins are a class of enzymes which catalytically transfer the ADP-ribosyl moiety of NAD into covalent linkage with se- lected acceptor amino acids on specific target proteins (TP).