• Corpus ID: 93998507

Bacterial toxins and virulence factors in disease

@inproceedings{Moss1995BacterialTA,
  title={Bacterial toxins and virulence factors in disease},
  author={Joel Moss and Barbara H. Iglewski and Martha Vaughan and Anthony T. Tu},
  year={1995}
}
Biosynthesis and targeting of pertussis toxin diphthamide - the toxin target in protein synthesis elogation factor 2 leukocidines heat-stable enterotoxin of escherichia coli therapeutic effects of botulinum toxins endotoxin - a mediator of and potential therapeutic target zot and ace toxins of vibrio cholerae ADP-ribosylation factors - a family of guanine nucleotide-binding proteins that activate cholera toxin and regulate vesicular transport liposomes and vehicles for vaccines GTP-binding… 
Proteolytic Activation of Cholera Toxin and Escherichia coli Labile Toxin by Entry into Host Epithelial Cells
TLDR
T84 cells express a serine-type protease(s) fully sufficient for activating the A subunits of CT and LT, however, the protease is only accessible for activation when the toxin enters the cell via the apical membrane.
Exploring the role of host cell chaperones/PPIases during cellular up-take of bacterial ADP-ribosylating toxins as basis for novel pharmacological strategies to protect mammalian cells against these virulence factors
  • H. Barth
  • Biology
    Naunyn-Schmiedeberg's Archives of Pharmacology
  • 2010
TLDR
Investigation of the cellular uptake of the binary actin ADP-ribosylating C2 toxin from Clostridium botulinum and the binary lethal toxin from Bacillus anthracis finds that Hsp90 and cyclophilin function selectively in promoting translocation of certain bacterial toxins depending on the enzyme domains of the individual toxins.
Structural Basis for the Differential Toxicity of Cholera Toxin and Escherichia coli Heat-labile Enterotoxin
TLDR
A comparison of the in vitro stability of two hybrid toxins, differing only in this 10-amino acid segment, revealed that the Ctx A2-segment conferred a greater stability to the interaction between the A- and B-subunits than the corresponding segment from E TX A2.
Escherichia coli K88ac Fimbriae Expressing Heat-Labile and Heat-Stable (STa) Toxin Epitopes Elicit Antibodies That Neutralize Cholera Toxin and STa Toxin and Inhibit Adherence of K88ac Fimbrial E. coli
TLDR
Data from this study demonstrated that K88ac fimbriae expressing LT and STa epitope antigens elicited neutralizing anti-toxin antibodies and anti-adhesin antibodies and suggested that E. coli fimbRIae could serve as a platform for the development of broad-spectrum vaccines against ETEC.
Molecular Biology of Actin-ADP-Ribosylating Toxins
TLDR
The actin cytoskeleton is the target of a large number of toxins, which leads to important cell dysfunctions and induces the severe lesions which are found in the associated pathologies.
Different Types of Cell Death Induced by Enterotoxins
TLDR
This article reviews the induction of the different types of cell death from various bacterial enterotoxins, including necrosis caused by pore-forming toxins, apoptotic signaling through cross-talk pathways involving mitochondrial damage, endoplasmic reticulum stress, and lysosomal injury.
Inactivation of the Elongation Factor Tu by Mosquitocidal Toxin-Catalyzed Mono-ADP-Ribosylation
TLDR
The inactivation of EF-Tu by MTX-mediated ADP-ribosylation and the resulting inhibition of bacterial protein synthesis are likely to play important roles in the cytotoxicity of the 27-kDa enzyme fragment of MTX toward E. coli.
Detoxification of Cholera Toxin without Removal of Its Immunoadjuvanticity by the Addition of (STa-related) Peptides to the Catalytic Subunit
TLDR
The addition of STa-related peptides to CTA reduced the toxicity of CT while partly preserving its natural immunoadjuvanticity, suggesting peptide extensions to CMA are a useful alternative to site-directed mutagenesis to detoxify CT.
Clostridium botulinum C2 toxin--new insights into the cellular up-take of the actin-ADP-ribosylating toxin.
TLDR
The mini-review describes main properties of C2 toxin and discusses new findings on the involvement of chaperones in the up-take process of the toxin.
Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen.
TLDR
It is reported here that short tracts of lysine, arginine, or histidine residues can also potentiate a protein for PA-dependent delivery to the cytosol and may aid in developing systems to deliver heterologous proteins and peptides to the cytoplasm of mammalian cells.
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