scholarly journals Isolation and function of a Clostridium perfringens enterotoxin fragment.

1987 ◽  
Vol 55 (12) ◽  
pp. 2912-2915 ◽  
Author(s):  
Y Horiguchi ◽  
T Akai ◽  
G Sakaguchi
Keyword(s):  
Clostridium Perfringens ◽  
Clostridium Perfringens Enterotoxin ◽  
And Function

scholarly journals Identification of a Claudin-4 Residue Important for Mediating the Host Cell Binding and Action of Clostridium perfringens Enterotoxin

2009 ◽  
Vol 78 (1) ◽  
pp. 505-517 ◽  
Author(s):  
Susan L. Robertson ◽  
James G. Smedley ◽  
Bruce A. McClane
Keyword(s):  
Host Cell ◽  
Clostridium Perfringens ◽  
Normal Structure ◽  
Structure And Function ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Extracellular Loop ◽  
Cell Binding ◽  
Clostridium Perfringens Enterotoxin ◽  
And Function

ABSTRACT The 24-member claudin protein family plays a key role in maintaining the normal structure and function of epithelial tight junctions. Previous studies with fibroblast transfectants and naturally sensitive Caco-2 cells have also implicated certain claudins (e.g., Claudin-4) as receptors for Clostridium perfringens enterotoxin (CPE). The present study first provided evidence that the second extracellular loop (ECL-2) of claudins is specifically important for mediating the host cell binding and cytotoxicity of native CPE. Rat fibroblast transfectants expressing a Claudin-4 chimera, where the natural ECL-2 was replaced by ECL-2 from Claudin-2, exhibited no CPE-induced cytotoxicity. Conversely, CPE bound to, and killed, CPE-treated transfectants expressing a Claudin-2 chimera with a substituted ECL-2 from Claudin-4. Site-directed mutagenesis was then used to alter an ECL-2 residue that invariably aligns as N in claudins known to bind native CPE but as D or S in claudins that cannot bind CPE. Transfectants expressing a Claudin-4N149D mutant lost the ability to bind or respond to CPE, while transfectants expressing a Claudin-1 mutant with the corresponding ECL-2 residue changed from D to N acquired CPE binding and sensitivity. Identifying carriage of this N residue in ECL-2 as being important for native CPE binding helps to explain why only certain claudins can serve as CPE receptors. Finally, preincubating CPE with soluble recombinant Claudin-4, or Claudin-4 fragments containing ECL-2 specifically blocked the cytotoxicity on Caco-2 cells. This result opens the possibility of using receptor claudins as therapeutic decoys to ameliorate CPE-mediated intestinal disease.

scholarly journals Innovative and Highly Sensitive Detection of Clostridium perfringens Enterotoxin Based on Receptor Interaction and Monoclonal Antibodies

Toxins ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 266
Author(s):  
Thea Neumann ◽  
Maren Krüger ◽  
Jasmin Weisemann ◽  
Stefan Mahrhold ◽  
Daniel Stern ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Clostridium Perfringens ◽  
Food Poisoning ◽  
Receptor Interaction ◽  
Clostridium Perfringens Enterotoxin ◽  
Fast Detection ◽  
Highly Sensitive ◽  
Basic And Applied Research ◽  
Highly Sensitive Detection

Clostridium perfringens enterotoxin (CPE) regularly causes food poisoning and antibiotic-associated diarrhea; therefore, reliable toxin detection is crucial. To this aim, we explored stationary and mobile strategies to detect CPE either exclusively by monoclonal antibodies (mAbs) or, alternatively, by toxin-enrichment via the cellular receptor of CPE, claudin-4, and mAb detection. Among the newly generated mAbs, we identified nine CPE-specific mAbs targeting five distinct epitopes, among them mAbs recognizing CPE bound to claudin-4 or neutralizing CPE activity in vitro. In surface plasmon resonance experiments, all mAbs and claudin-4 revealed excellent affinities towards CPE, ranging from 0.05 to 2.3 nM. Integrated into sandwich enzyme-linked immunosorbent assays (ELISAs), the most sensitive mAb/mAb and claudin-4/mAb combinations achieved similar detection limits of 0.3 pg/mL and 1.0 pg/mL, respectively, specifically detecting recombinant CPE from spiked feces and native CPE from 30 different C. perfringens culture supernatants. The implementation of mAb- and receptor-based ELISAs into a mobile detection platform enabled the fast detection of CPE, which will be helpful in clinical laboratories to diagnose diarrhea of assumed bacterial origin. In conclusion, we successfully employed an endogenous receptor and novel high affinity mAbs for highly sensitive and specific CPE-detection. These tools will be useful for both basic and applied research.

Prevalence of Clostridium perfringens , Clostridium perfringens enterotoxin and dysbiosis in fecal samples of dogs with diarrhea

2014 ◽  
Vol 174 (3-4) ◽  
pp. 463-473 ◽  
Author(s):  
Yasushi Minamoto ◽  
Naila Dhanani ◽  
Melissa E. Markel ◽  
Jörg M. Steiner ◽  
Jan S. Suchodolski
Keyword(s):  
Clostridium Perfringens ◽  
Clostridium Perfringens Enterotoxin ◽  
Fecal Samples

Synthesis, 18F-labelling and radiopharmacological characterisation of the C-terminal 30mer of Clostridium perfringens enterotoxin as a potential claudin-targeting peptide

Amino Acids ◽  
2018 ◽  
Vol 51 (2) ◽  
pp. 219-244
Author(s):  
Reik Löser ◽  
Miriam Bader ◽  
Manuela Kuchar ◽  
Robert Wodtke ◽  
Jens Lenk ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Clostridium Perfringens Enterotoxin ◽  
Targeting Peptide ◽  
18F Labelling

scholarly journals Using More Than 1 (Path)Way to Kill a Host Cell: Lessons From Clostridium perfringens Enterotoxin

2020 ◽  
Vol 13 ◽  
pp. 117863612093151
Author(s):  
Bruce McClane ◽  
Archana Shrestha
Keyword(s):  
Recent Work ◽  
Clostridium Perfringens ◽  
Caspase 3 ◽  
Kinase Domain ◽  
Intermediate Step ◽  
Clostridium Perfringens Enterotoxin ◽  
Mixed Lineage Kinase ◽  
Intestinal Infections ◽  
Apoptosis And Necrosis

Clostridium perfringens enterotoxin (CPE) is responsible for the symptoms of common intestinal infections due to C. perfringens type F isolates. CPE is a pore-forming toxin that uses certain claudins as a receptor. Previous studies showed that, in enterocyte-like Caco-2 cells, low CPE concentrations cause caspase 3-mediated apoptosis but high CPE concentrations cause necrosis. The recent work published in mBio by Shrestha, Mehdizadeh Gohari, and McClane determined that RIP1 and RIP3 are involved in both CPE-mediated apoptosis and necrosis in Caco-2 cells. Furthermore, mixed lineage kinase-domain (MLKL) oligomerization was shown to be important for necrosis caused by CPE, identifying this necrosis as programmed necroptosis. In addition, calpain activation due to Ca2+ influx through the CPE pore was identified as a critical intermediate step for MLKL oligomerization and, thus, CPE-induced necroptosis. These findings may have applicability to understand the action of some other pore-forming toxins that induce necroptosis and may also be important for understanding CPE action in vivo.

Evidence for Clostridium perfringens Enterotoxin (CPE) Inducing a Mitogenic and Cytokine Response In Vitro and a Cytokine Response In Vivo

1999 ◽  
Vol 38 (2) ◽  
pp. 96-100 ◽  
Author(s):  
F. Morgan Wallace ◽  
Annette S. Mach ◽  
Andreas M. Keller ◽  
James A. Lindsay
Keyword(s):  
Clostridium Perfringens ◽  
Cytokine Response ◽  
Clostridium Perfringens Enterotoxin
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