Just, Actin‐ADP‐Ribosylating Toxins: Cytotoxic Mechanisms of Clostridium botulinum C2 Toxin and Clostridium perfringens lota Toxin, Bacterial Toxins, 10.1002/9783527614615, (93-101), (2008). Wiley Online Library

Bakteriella toxiner — Vidare har C. Botulinum C3 ADP-ribosylater GTP-bindande proteiner Rho och Ras och Pertussis-toxin ADP-Ribosylates Gi

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 . The C2-like toxins from Clostridium sp. [44,250] and the newly characterized SpvB from Salmonella sp. Se hela listan på fr.wikipedia.org It is well known that a number of toxins produced by bacteria exert their action by ADP-ribosylating reaction to certain proteins which are essential for normal eukaryotic cellular functions.

Here we studied the proteolytic activation of the ADP-ribosyltransferase activity of MTX. ADP-ribosylation is a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins. Poly (ADP)-ribosyltransferase 1 (PARP-1) was cleaved in C2 toxin-treated cells, an indication of caspase 3 activation and a hallmark of apoptosis. Furthermore, specific caspase inhibitors prevented C2 toxin-induced apoptosis, implying that caspases 8 and 9 were activated in C2 toxin-treated cells. The airway pathogen Mycoplasma pneumoniae(Mp) produces a virulence factor with ADP-ribosyltransferase and vacuolating activities known as Community-Acquired Respiratory Distress Syndrome Toxin (CARDS TX). Ui M. (1990) Pertusis toxin as a valuable probe for G-protein involvement in signal transduction, in ADP-Ribosylating Toxins and G-proteins: Insights into Signal Transduction (Moss J. and Vaughan M., eds.), American Society for Microbiology, Washington, D.C., pp. 45–77. Google Scholar 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). However, these toxins, which modify actin

Köp boken ADP-Ribosylating Toxins (ISBN 9783642769689) hos Adlibris.

2017-09-06

There are two principal reasons for the broad and still growing ADP-ribosylating toxins have been the focus of intensive research for more than 30 years. Researchers from diverse fields of science have taken an interest in these bacterial toxins; they are studied, for example, by microbiologists, biochemists, cell biologists, and pharmacologists. There are two principal reasons for the broad and still growing We show that the unique bacterial ADP-ribosylating and vacuolating toxin produced by Mycoplasma pneumoniae and designated community-acquired respiratory distress syndrome (CARDS) toxin activates the NLRP3 inflammasome by colocalizing with the NLRP3 inflammasome and catalyzing the ADP-ribosylation of NLRP3. Clostridium botulinum C2 toxin, the prototype of the family of binary actin ADP-ribosylating toxins, mono-ADP-ribosylates G-actin at Arg-177 (1).

ADP-ribosylating toxins have been the focus of intensive research for more than 30 years. Researchers from diverse fields of science have taken an interest in these bacterial toxins; they are studied, for example, by microbiologists, biochemists, cell biologists, and pharmacologists. There are two principal reasons for the broad and still growing

av D Pullirsch · 2010 · Citerat av 72 — not only permeable for Ca2+ but also highly permeable for toxic.

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(A) Structure-based alignment of ADP-ribosylating toxins from the cholera (CTxg) and diphtheria toxin (DTxg) subgroups.

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.
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The structure of BECa shows striking resemblance with other binary actin ADP-ribosylating toxins (ADPRTs), especially in terms of its overall protein fold and mechanisms of substrate recognition. We present a detailed picture of interactions between BECa and NADH, including bound water molecules located near the C1'-N glycosidic bond of NADH and the catalytically important ADP-ribosylating

The mosquitocidal toxin (MTX) from Bacillus sphaericus SSII-1 is a ∼97-kDa protein sharing sequence homology within the N terminus with the catalytic domains of various bacterial ADP-ribosyltransferases. Here we studied the proteolytic activation of the ADP-ribosyltransferase activity of MTX. ADP-ribosylation is a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins. Poly (ADP)-ribosyltransferase 1 (PARP-1) was cleaved in C2 toxin-treated cells, an indication of caspase 3 activation and a hallmark of apoptosis. Furthermore, specific caspase inhibitors prevented C2 toxin-induced apoptosis, implying that caspases 8 and 9 were activated in C2 toxin-treated cells. The airway pathogen Mycoplasma pneumoniae(Mp) produces a virulence factor with ADP-ribosyltransferase and vacuolating activities known as Community-Acquired Respiratory Distress Syndrome Toxin (CARDS TX). Ui M. (1990) Pertusis toxin as a valuable probe for G-protein involvement in signal transduction, in ADP-Ribosylating Toxins and G-proteins: Insights into Signal Transduction (Moss J. and Vaughan M., eds.), American Society for Microbiology, Washington, D.C., pp. 45–77.