Efficient production of heat-labile enterotoxin mutant proteins by overexpression of dsbA in a degP-deficient Escherichia coli strain |
| |
Authors: | C Wülfing R Rappuoli |
| |
Institution: | (1) IRIS, Chiron Vaccines Immunobiological Research Institute Siena, Via Fiorentina 1, 53100 Siena, Italy Tel. +39-577-243414; Fax +39-577-243564 e-mail rappuoli@iris02.biocine.it, IT |
| |
Abstract: | Escherichia coli heat-labile enterotoxin (LT) mutants containing Val60→Gly or Ser114→Lys substitutions in the A subunit do not produce the A subunit efficiently in E. coli. These mutants accumulate mostly the B pentamer devoid of the A subunit in the periplasmic space. Here we show that overproduction
of the periplasmic chaperone DsbA, which is involved in disulfide bond formation, in a strain deficient in the periplasmic
protease DegP allows efficient production of the mutant LT molecules. Our results suggest that the formation of the oligomeric
toxin is influenced by DsbA, which helps protein folding, and by DegP, which removes the folded intermediates that can be
untoxic for the cell.
Received: 30 October 1996 / Accepted: 8 January 1997 |
| |
Keywords: | LT CT Escherichia coli enterotoxin DsbA Protein folding Bacterial toxin Cholera Enterotoxigenic E coli Chaperones Disulfide bridge |
本文献已被 SpringerLink 等数据库收录! |
|