Engineering of cholera toxin A-subunit for carriage of epitopes at its amino end

FEBS Letters
J SanchezA Buelna

Abstract

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.

References

Mar 23, 1976·Biochemistry·D M Gill
Sep 1, 1990·Research in Microbiology·J SanchezJ Holmgren
Apr 29, 1997·Proceedings of the National Academy of Sciences of the United States of America·I BergerotC Thivolet

❮ Previous
Next ❯

Related Concepts

Related Feeds

Avian Influenza: Innate Immune Adjuvant (ASM)

Adjuvants systems that are added to vaccines against avian influenza have be explored to enhance the innate immune system response against the virus. Here is the latest research on avian influenza and the innate immune adjuvant.

Avian Influenza: Innate Immune Adjuvant

Adjuvants systems that are added to vaccines against avian influenza have be explored to enhance the innate immune system response against the virus. Here is the latest research on avian influenza and the innate immune adjuvant.