2006
DOI: 10.3748/wjg.v12.i8.1229
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Cloning of α-β fusion gene from Clostridium perfringens and its expression

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Cited by 9 publications
(3 citation statements)
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“…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. Another chimeric antigen with ETX and CPB (rETXCPB) was able to generate titers of 6 and 10 IU/mL against the respective toxins in rabbits [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. Another chimeric antigen with ETX and CPB (rETXCPB) was able to generate titers of 6 and 10 IU/mL against the respective toxins in rabbits [71].…”
Section: Beta Toxin (Cpb)mentioning
confidence: 99%
“…It may be possible to create targeted vaccine(s) composed of non‐toxic peptides. That seems feasible, as all C perfringens toxins genes have been cloned and expressed as recombinant proteins (α: Bennett and others 1999, Schoepe and others 2006 ; β: Steinthorsdottir and others 1995 ; α‐β: Bai and others 2006 ; β‐β2: Xu and others 2005 ; ϵ: Goswami and others 1996, Oyston and others 1998 ; ι: Sirard and others 1997 ; enterotoxin: Belyi and Varfolomeeva 2003 ; β2, Gibert and others 1997, Lebrun and others 2007). Another way would be to select strains producing naturally protective immunogenic but non‐toxic variants of the toxins of interest, such as the 1121A/19 strain of C perfringens , which produces a non‐toxic variant of a toxin that induces a protective response against different toxic variants of α (Schoepe and others 2001).…”
Section: Prophylaxismentioning
confidence: 99%
“…When these histidines are replaced by other amino acid residues, such as glycine, the hemolytic activity and lethality of the α-toxin are significantly reduced or even eliminated. Nonetheless, its antigenicity can be retained [12][13][14], pointing to a promising strategy for the development of a subunit vaccine against C. perfringens α-toxin [15,16].…”
Section: Introductionmentioning
confidence: 99%