Premium
Carrier Potential Properties of Bacillus thuringiensis Cry1A Toxins for a Diphtheria Toxin Epitope
Author(s) -
Guerrero G. G.,
MorenoFierros L.
Publication year - 2007
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2007.01992.x
Subject(s) - diphtheria toxin , immunogenicity , toxin , epitope , bacillus thuringiensis , recombinant dna , biology , diphtheria , antibody , immunization , microbiology and biotechnology , corynebacterium diphtheriae , amino acid , chemistry , biochemistry , virology , gene , immunology , bacteria , genetics , vaccination
The N‐terminal half or toxic fragment of Bacillus thuringiensis Cry proteins is comprised of three structural domains. In a previous paper, we showed that this region plays an important role in the immunogenicity of the B. thuringiensis Cry proteins. Due to this ability and along with their stability it is worthy of investigating whether this region has carrier potential. To approach this, an eight amino acid hydrophobic motif in α‐helix 7 of wild‐type (WT) Cry1A toxins was exchanged for a diphtheria toxin epitope (DTB). The resultant recombinant toxins were tested for their ability to induce specific anti‐Cry and anti‐diphtheria toxin antibodies in mice after intraperitoneal and nasal immunization. We found that recombinant Cry1A toxins retained their ability to induce serum and mucosal anti‐Cry Ab as well as IgG subclasses, although with a varied magnitude. By the systemic route, the effect of the amino acid substitution in the ratio of the IgG1/IgG2a Ab, leading in some sites toward IgG1 or IgG2a is more evident. Interestingly, mice produced specific anti‐DTB IgG, and IgA after intranasal immunization. Together, our results support and show the immunogenic properties of the WT Cry1A toxins as well as its carrier potential for a DTB.