Generation and characterization of recombinant bivalent fusion protein r-Cpib for immunotherapy against Clostridium perfringens beta and iota toxemia

Das, Shreya; Majumder, Saugata; Kingston, Joseph J.; Batra, Harsh Vardhan

doi:10.1016/j.molimm.2015.12.001

Cited by 11 publications

(5 citation statements)

References 27 publications

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“…The existing literature describes how it is possible to overcome this problem through the use of a chimeric antigen to improve the solubility of the antigen. As described previously, both the rETXCPB and rCPIB contain CPB, or part of it, in the C -terminal region, having soluble proteins at the end [70,71]. However, in the same study, both the rCPAB2B1 and the rCPA that were produced during the research were insoluble [26].…”

Section: Beta Toxin (Cpb)mentioning

confidence: 68%

“…Further studies have focused on determining the toxicity mechanism of CPB and have generated important recommendations for vaccinology specialists that have facilitated the development of recombinant vaccines [61,62,63,64]. Of the various strategies that are used to develop recombinant vaccines containing CPB, four approaches, in particular, are worth highlighting: (1) the insertion of point mutations for the generation of toxoids; (2) the expression of the whole toxin sequence; (3) the expression of its C -terminal domain (CPB-C (143–311) ); and (4) the expression of chimeric antigens containing other toxins (e.g., CPA, CPB2, or ETX) or the B subunit of the heat-labile enterotoxin of E. coli (LTB) (Table 3) [18,26,65,66,67,68,69,70,71]. …”

Section: Beta Toxin (Cpb)mentioning

confidence: 99%

“…A study with the region CPB (143–311) , which was fused to the C -terminal part of CPI (CPI-C (466–665) ), showed that the resulting protein (called rCPIB) was able to protect 83% and 91% of mice challenged with 5 × LD 100 of CPI and CPB, respectively [70]. Similarly, Bai et al [73] produced a bivalent chimera that contained CPA and CPB (rCPAB), which was able to protect 100% (10/10) of mice challenged with 1 L+ of CPB.…”

Section: Beta Toxin (Cpb)mentioning

confidence: 99%

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Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines

Ferreira

Moreira

Cunha

et al. 2016

Toxins

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Clostridium perfringens is a spore-forming, commensal, ubiquitous bacterium that is present in the gastrointestinal tract of healthy humans and animals. This bacterium produces up to 18 toxins. The species is classified into five toxinotypes (A–E) according to the toxins that the bacterium produces: alpha, beta, epsilon, or iota. Each of these toxinotypes is associated with myriad different, frequently fatal, illnesses that affect a range of farm animals and humans. Alpha, beta, and epsilon toxins are the main causes of disease. Vaccinations that generate neutralizing antibodies are the most common prophylactic measures that are currently in use. These vaccines consist of toxoids that are obtained from C. perfringens cultures. Recombinant vaccines offer several advantages over conventional toxoids, especially in terms of the production process. As such, they are steadily gaining ground as a promising vaccination solution. This review discusses the main strategies that are currently used to produce recombinant vaccines containing alpha, beta, and epsilon toxins of C. perfringens, as well as the potential application of these molecules as vaccines for mammalian livestock animals.

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Section: Beta Toxin (Cpb)mentioning

confidence: 68%

Section: Beta Toxin (Cpb)mentioning

confidence: 99%

Section: Beta Toxin (Cpb)mentioning

confidence: 99%

See 1 more Smart Citation

Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines

Ferreira

Moreira

Cunha

et al. 2016

Toxins

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“…The most important of these virulence factors are phospholipase C known as Alpha-toxin, β-pore forming toxin, NetB, and a zinc metallopeptidase protein [7,8,28]. Utilizing a fusion of non toxic variants of these proteins as a recombinant subunit vaccine candidate could enhance protective immunity [31,6]. 6 http://vacres.pasteur.ac.ir…”

Section: Introductionmentioning

confidence: 99%

“…Utilizing a fusion of non toxic variants of these proteins as a recombinant subunit vaccine candidate could enhance protective immunity [31,6]. 6 http://vacres.pasteur.ac.ir…”

Section: Introductionmentioning

confidence: 99%

Design and Expression Optimization of a Chimeric Derivative of NetB, Alpha-Toxin and Metallopeptidase Proteins as a Subunit Vaccine Against Clostridium perfringens

Katalani¹,

Nematzadeh

Ahmadian

et al. 2019

vacres

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Avian necrotic enteritis (NE) is a multi-virulence disease caused by the bacterium Clostridium perfringens. Several toxins of this bacteria are components of different candidate vaccines, and have been considered as important factors in pathogenesis of NE. A fusion subunit protein composed of immunodominant segments of NetB, Alpha-toxin and metallopeptidase proteins (NAM) was designed. The high level production of NE subunit vaccine candidate is important for the in vitro and in vivo evaluation and later to decrease the production costs. Therefore, the Response Surface Methodology (RSM) was used for optimizing E. coli culture condition. To this end, induction conditions including cell optical density prior induction (OD600nm), IPTG concentration, post-induction temperature and time were modified. The statistical analysis revealed that all variables except IPTG had significant effects on production and solubility of rNAM. A 7.39 fold increase in production of soluble rNAM was achieved when the post induction temperature, IPTG concentration, the pre-induction OD and time were 19 ºC, 0.55 mM, 0.8 respectively in 8 h after induction. Our study indicated that the RSM method is a simple and superior strategy for protein expression improvement which is considered as a major limitation in production of vaccine candidate and other recombinant proteins using different hosts. Katalani1 et al Design and Expression Optimization of a Chimeric … * Recombinant NAM concentration yield (mg/L) obtained from densitometry analysis with different expression conditions of IPTG concentration, OD600, temperature and induction time using a central composite design for four variables.

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Clostridial Binary Toxins: Basic Understandings that Include Cell Surface Binding and an Internal “Coup de Grâce”

Stiles

2016

Current Topics in Microbiology and Immunology

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Clostridium species can make a remarkable number of different protein toxins, causing many diverse diseases in humans and animals. The binary toxins of Clostridium botulinum, C. difficile, C. perfringens, and C. spiroforme are one group of enteric-acting toxins that attack the actin cytoskeleton of various cell types. These enterotoxins consist of A (enzymatic) and B (cell binding/membrane translocation) components that assemble on the targeted cell surface or in solution, forming a multimeric complex. Once translocated into the cytosol via endosomal trafficking and acidification, the A component dismantles the filamentous actin-based cytoskeleton via mono-ADP-ribosylation of globular actin. Knowledge of cell surface receptors and how these usurped, host-derived molecules facilitate intoxication can lead to novel ways of defending against these clostridial binary toxins. A molecular-based understanding of the various steps involved in toxin internalization can also unveil therapeutic intervention points that stop the intoxication process. Furthermore, using these bacterial proteins as medicinal shuttle systems into cells provides intriguing possibilities in the future. The pertinent past and state-of-the-art present, regarding clostridial binary toxins, will be evident in this chapter.

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Generation and characterization of recombinant bivalent fusion protein r-Cpib for immunotherapy against Clostridium perfringens beta and iota toxemia

Cited by 11 publications

References 27 publications

Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines

Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines

Design and Expression Optimization of a Chimeric Derivative of NetB, Alpha-Toxin and Metallopeptidase Proteins as a Subunit Vaccine Against Clostridium perfringens

Clostridial Binary Toxins: Basic Understandings that Include Cell Surface Binding and an Internal “Coup de Grâce”

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