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

FEBS Letters

Buelna, A¹  Sanchez, J¹  Argotte, R¹ 

[1] Centro de Investigación sobre Enfermedades Infecciosas, Instituto Nacional de Salud Publica, Av Universidad 655, Col. Sta. Maria Ahuacatitlan, Cuernavaca, Morelos 62508, Mexico

关键词: Fusion protein;    Heat-stable enterotoxin;    E. coli;    Mucosal immunoadjuvant;    Toxin assembly;    Toxin active site;   

DOI  :  10.1016/S0014-5793(96)01445-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown