View this table: In this window In a new window. Table 1. Bacterial enzymatic toxins acting on host cell cytosolic factors. Previous Section. The adenylate cyclase toxins. Crit Rev Microbiol 30 : — CrossRef Medline Google Scholar.
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Aktories K Aktories K. Bacterial protein toxins that modify host regulatory GTPases. Nat Rev Microbiol 9 : — Botulinum C2 toxin ADP-ribosylates actin. Nature : — Actin as target for modification by bacterial protein toxins. FEBS J : — Immunity 35 : 34 — The comprehensive sourcebook of bacterial protein toxins , 3rd ed. Elsevier , Amsterdam, The Netherlands. Google Scholar. Membrane injury by pore-forming proteins. Curr Opin Cell Biol 21 : — Tetanus toxin is transported in a novel neuronal compartment characterized by a specialized pH regulation. J Biol Chem : — Regulation of innate immunity by Rho GTPases.
Trends Cell Biol 15 : — Trends Cell Biol 13 : — Induction of transient macroapertures in endothelial cells through RhoA inhibition by Staphylococcus aureus factors. J Cell Biol : — Pathogen-derived effectors trigger protective immunity via activation of the Rac2 enzyme and the IMD or Rip kinase signaling pathway. Immunity 35 : — Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins.
Cell Mol Life Sci 65 : — Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin. Haploid genetic screens in human cells identify host factors used by pathogens. Science : — Gangliosides as high affinity receptors for tetanus neurotoxin. Anthrax toxin. Annu Rev Cell Dev Biol 19 : 45 — Microbial and viral pathogens in colorectal cancer. Lancet Oncol 12 : — Cossart P Cossart P. Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes.
Proc Natl Acad Sci : — A Burkholderia pseudomallei toxin inhibits helicase activity of translation factor eIF4A. Ubiquitin-binding domains—From structures to functions. Nat Rev Mol Cell Biol 10 : — SV2 is the protein receptor for botulinum neurotoxin A. Cell : — Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest. Mol Microbiol 37 : — Bacterial protein toxins: Current and potential clinical use.
Curr Med Chem 15 : — Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. Common themes in the design and function of bacterial effectors.
Cell Host Microbe 5 : — The biology of the cytolethal distending toxins. Toxins Basel 3 : — Infect Immun 79 : — Genetic diversity among botulinum neurotoxin-producing clostridial strains. J Bacteriol : — Rho GTPases: Biochemistry and biology. Annu Rev Cell Dev Biol 21 : — Shiga toxins—From cell biology to biomedical applications. Nat Rev Microbiol 8 : — Glucosylation of Rho proteins by Clostridium difficile toxin B. Antiinflammatory cAMP signaling and cell migration genes co-opted by the anthrax bacillus. A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein.
Breaking the wall: Targeting of the endothelium by pathogenic bacteria. Nat Rev Microbiol 8 : 93 — Medline Google Scholar. Rho GTPase-activating bacterial toxins: From bacterial virulence regulation to eukaryotic cell biology. Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc Natl Acad Sci 79 : — Cell Host Microbe 10 : — Vaccine 23 : — Aepfelbacher, M.
Mohammadi, S. Michaelson, D. Rac1 accumulates in the nucleus during the G2 phase of the cell cycle and promotes cell division. Lanning, C. The Rac1 C-terminal polybasic region regulates the nuclear localization and protein degradation of Rac1. Bourguignon, L. CD44 interaction with Tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. Brugirard-Ricaud, K. Site-specific antiphagocytic function of the Photorhabdus luminescens type III secretion system during insect colonization.
Dowen, R. A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes. Oswald, E. Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers. USA 91 , — A single protein of kDa is associated with the multinucleating and necrotizing activity coded by the Vir plasmid of Escherichia coli. Stoll, T. A new member of a growing toxin family — Escherichia coli cytotoxic necrotizing factor 3 CNF3.
Toxicon 54 , — Lockman, H. Yersinia pseudotuberculosis produces a cytotoxic necrotizing factor. Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Kim, K. Blumenthal, B. The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol. Knust, Z. Cleavage of Escherichia coli cytotoxic necrotizing factor 1 is required for full biologic activity.
Schmidt, G. Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor 1. Flatau, G.
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Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. The identification of deamidation as a novel molecular mechanism of Cnf proteins along with work in reference Buetow, L. Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1. The first structural insights into deamidation catalysed by Cnf proteins.
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Lerm, M. Identification of the region of Rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 CNF1. Falzano, L. Interaction of Escherichia coli cytotoxic necrotizing factor type 1 CNF1 with cultured cells. Cytotechnology 11 , S56—S58 Cytotoxic effect of multinucleation in HeLa cell cultures associated with the presence of Vir plasmid in Escherichia coli strains. Denko, N. Uncoupling of S-phase and mitosis by recombinant cytotoxic necrotizing factor 2 CNF2.
Cell Res. Malorni, W. Hoffmann, C. Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac. Doye, A. An in-depth analysis of the degradation of RHO-family proteins after Cnf1 treatment. Horiguchi, Y. Purification and characterization of Bordetella bronchiseptica dermonecrotic toxin.
Fukui-Miyazaki, A. Bordetella dermonecrotic toxin binds to target cells via the N-terminal 30 amino acids. Matsuzawa, T. Bordetella dermonecrotic toxin undergoes proteolytic processing to be translocated from a dynamin-related endosome into the cytoplasma in an acidification-independent manner.
Masuda, M. Activation of Rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin. The identification of the substrates for the transglutaminase activity of Dnt. The Rho-deamidating cytotoxic-necrotizing factor CNF1 from Escherichia coli possesses transglutaminase activity.
Cysteine and histidine are essential for enzyme activity. Cassel, D. Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. USA 75 , — A classical paper on the molecular mechanism of cholera toxin. Lax, A. The Pasteurella multocida toxin interacts with signalling pathways to perturb cell growth and differentiation. Orth, J. Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation. A seminal paper on the identification of Pmt as a deamidase. Majumdar, S. Coleman, D. Van Dop, C.
Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. Freissmuth, M. Sprang, S. G protein mechanisms: insights from structural analysis. An excellent early review on structure—function analyses of G proteins. Wilson, B. Modulation of host cell gene expression through activation of STAT transcription factors by Pasteurella multocida toxin.
Preuss, I. Pasteurella multocida toxin is a potent activator of anti-apoptotic signalling pathways. Rozengurt, E. Pasteurella multocida toxin: potent mitogen for cultured fibroblasts. USA 87 , — Staddon, J. An early study identifying the action of Pmt. Zywietz, A. Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. Involvement of Gq but not G The introduction of gene deletions in Pmt studies.
Hofmann, F. Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. Greco, A. Carbohydrate recognition by Clostridium difficile toxin A. Egerer, M. Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on a cysteine protease activity. Genisyuerek, S. Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B.
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Reineke, J. Autocatalytic cleavage of Clostridium difficile toxin B. The identification of InsP 6 as an essential cofactor for the processing of clostridial glucosylating toxins. Pfeifer, G. Cellular uptake of Clostridium difficile toxin B: translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. Pruitt, R. Structural organization of the functional domains of Clostridium difficile toxins A and B.
An impressive study on the power of negative-stain microscopy and three-dimensional restructuring for the structure—function analysis of clostridial toxins. Milligan, G. Heterotrimeric G-proteins: a short history. Kitadokoro, K.
Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin. Upadhyay, A. Huang, Z. Subversion of actin dynamics by EspM effectors of attaching and effacing bacterial pathogens. Sixma, T. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. A seminal paper on the structure of cholera toxin.
Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln of the GTP-binding protein Rho. USA 94 , — Gierschik, P. ADP-ribosylation of signal-transducing guanine nucleotide-binding proteins by pertussis toxin. Large clostridial cytotoxins. Download references. The work from the K. GTP-binding proteins that have GTP hydrolysis activity and act as molecular switches, dependent on the bound nucleotide GDP-bound proteins are in the off state, and GTP-bound proteins are in the on state.
The carboxy-terminal tail of the protein to which an isoprenyl moiety has been attached at the carboxy-terminal cysteine residue as a post-translational modification. A C 20 isoprenyl moiety geranylgeranyl is usually attached to RHO-family proteins. ADP-ribosylating factor. A family of small GTPases that are involved in membrane and vesicle traffic. It inhibits the microtubule -mediated secretory pathway and alters cytoskeleton organization in polarized epithelial cells.
It has been identified as the viral enterotoxin based on the observation that the protein caused diarrhea when administered intraperitoneally or intra-ileally in infant mice in an age-dependent manner. From Wikipedia, the free encyclopedia.
Caister Academic Press. Retrieved In Proft T ed.
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