<i>Clostridium perfringens</i>type C isolates rapidly upregulate their toxin production upon contact with host cells

McClane, Bruce A.

doi:10.4161/viru.1.2.10679

Cited by 12 publications

(13 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…␤-Toxin was also found to be required for C. perfringens-induced necrotic enteritis in rabbit ileal loops, whereas PFO and (non-PFT) alpha-toxin were not (406). It is not known whether this was caused by direct effects of the PFT on the intestinal cells or indirectly, via, for example, the immune system.…”

Section: Pft-induced Barrier Dysfunctionmentioning

confidence: 91%

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

Los

Randis

Aroian

et al. 2013

Microbiol Mol Biol Rev

350

351

View full text Add to dashboard Cite

SUMMARY Pore-forming toxins (PFTs) are the most common bacterial cytotoxic proteins and are required for virulence in a large number of important pathogens, including Streptococcus pneumoniae , group A and B streptococci, Staphylococcus aureus , Escherichia coli , and Mycobacterium tuberculosis . PFTs generally disrupt host cell membranes, but they can have additional effects independent of pore formation. Substantial effort has been devoted to understanding the molecular mechanisms underlying the functions of certain model PFTs. Likewise, specific host pathways mediating survival and immune responses in the face of toxin-mediated cellular damage have been delineated. However, less is known about the overall functions of PFTs during infection in vivo . This review focuses on common themes in the area of PFT biology, with an emphasis on studies addressing the roles of PFTs in in vivo and ex vivo models of colonization or infection. Common functions of PFTs include disruption of epithelial barrier function and evasion of host immune responses, which contribute to bacterial growth and spreading. The widespread nature of PFTs make this group of toxins an attractive target for the development of new virulence-targeted therapies that may have broad activity against human pathogens.

show abstract

Section: Pft-induced Barrier Dysfunctionmentioning

confidence: 91%

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

Los

Randis

Aroian

et al. 2013

Microbiol Mol Biol Rev

350

351

View full text Add to dashboard Cite

show abstract

“…It has been reported that a monoclonal antibody against a particular B-cell epitope may provide sufficient protection from enterotoxemia. (Percival et al 1990;McClane 2010). The location of the epitope, recognized by the protective monoclonal antibody, has been mapped to amino acids 134-145 (peptide sequence SFANTNTNTNSK) and has been found to overlap the putative membrane inserting loop.…”

Section: Discussionmentioning

confidence: 99%

Immunogenicity assessment of Clostridium perfringens type D epsilon toxin epitope-based chimeric construct in mice and rabbit

et al. 2020

View full text Add to dashboard Cite

Epsilon toxin (Etx) belongs to family of pore-forming toxin and is produced by Clostridium perfringens type D. The Etx toxin is responsible for the pathogenesis of enterotoxaemia in sheep and goats, and occasionally in other livestock animals. The present study aimed to develop a Clostridium perfringens epsilon toxin-based chimeric epitope construct having immunodominant B-cell epitope and universal T-cell epitope and its immunogenicity was evaluated in mice and rabbit. An artificial chimeric epitope construct (CEC) was prepared by joining tandem repeats of a peptide containing amino acids (aa) 134-145 of epsilon toxin B-cell epitope and universal T-cell epitopes. The CEC was expressed in the Escherichia coli following codon optimization for efficient translational efficiency and purified by affinity chromatography. The antigenic reactivity of r-CEC proteins was confirmed by western blot with rabbit anti-r-Etox hyperimmune sera. The immunogenicity of the recombinant single CEC was examined in mice and rabbit by indirect ELISA. It was found that r-CEC yielded high titers of neutralizing antibodies (≥ 1.035 IU/ml) in immunized mice and rabbit. The potency of chimeric protein immunized serum was observed to be higher than the recommended level (0.1-0.3 IU/ml) for protection in sheep and goats. This indicated the potential ability of the chimeric protein as a vaccine candidate. This further requires studying the immune response in targeted host species (sheep and goat).

show abstract

“… 11 C. prefringens is able to produce biofilm on cell surfaces and the presence of pili as well as the production of sialidase can collaborate with this process. 12 McClane 13 showed that adherent C. perfringens strains increase the neuraminidase and toxin production.…”

mentioning

confidence: 99%

Adhesion and invasion of Clostridium perfringens type A into epithelial cells

Llanco

Nakano

Moraes

et al. 2017

Brazilian Journal of Microbiology

View full text Add to dashboard Cite

Clostridium perfringens is the causative agent for necrotic enteritis. It secretes the major virulence factors, and α- and NetB-toxins that are responsible for intestinal lesions. The TpeL toxin affects cell morphology by producing myonecrosis, but its role in the pathogenesis of necrotic enteritis is unclear. In this study, the presence of netB and tpeL genes in C. perfringens type A strains isolated from chickens with necrotic enteritis, their cytotoxic effects and role in adhesion and invasion of epithelial cells were evaluated. Six (27.3%) of the 22 C. perfringens type A strains were harboring the tpeL gene and produced morphological alterations in Vero cells after 6 h of incubation. Strains tpeL (−) induced strong cell rounding after 6 h of incubation and produced cell enlargement. None of the 22 strains harbored netB gene. All the six tpeL (+) gene strains were able to adhere to HEp-2 cells; however, only four of them (66.6%) were invasive. Thus, these results suggest that the presence of tpeL gene or TpeL toxin might be required for the adherence of bacteria to HEp-2 cells; however, it could not have any role in the invasion process.

show abstract

Clostridium perfringenstype C isolates rapidly upregulate their toxin production upon contact with host cells

Cited by 12 publications

References 18 publications

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

Immunogenicity assessment of Clostridium perfringens type D epsilon toxin epitope-based chimeric construct in mice and rabbit

Adhesion and invasion of Clostridium perfringens type A into epithelial cells

Contact Info

Product

Resources

About