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Engineering of cholera toxin A‐subunit for carriage of epitopes at its amino end
Author(s) -
Sanchez J,
Argotte R,
Buelna A
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01445-7
Subject(s) - cholera toxin , complementation , recombinant dna , epitope , protein subunit , toxin , chemistry , enterotoxin , fusion protein , antibody , biochemistry , microbiology and biotechnology , biology , escherichia coli , immunology , phenotype , gene
The cholera toxin A‐subunit (CTA) was genetically engineered at its amino end and tested for carriage of epitopes by fusion of the STa heat‐stable enterotoxin analogue CAELCCNPAC. Efficient holotoxin formation by complementation in trans with cholera toxin B‐subunit (CTB) indicated no decrease in affinity for CTB but evidence of reduced toxicity suggests steric interference by the decapeptide with the active site. The holotoxin was stable, able to bind to GM1 and was recognized by anti‐STa and anti‐CTA antibodies. The use of a full‐length CTA might have been a key step for successful genetic fusions. Based on these findings, it seems worthwhile pursue the development of CTA for construction of recombinant mucosal immunoadjuvants.