Conformational integrity of a recombinant toxoid of Pseudomonas aeruginosa exotoxin A containing a deletion of glutamic acid-553.
Biochim Biophys Acta
; 1138(2): 162-6, 1992 Feb 14.
Article
de En
| MEDLINE
| ID: mdl-1347236
ABSTRACT
A mutant form of Pseudomonas aeruginosa exotoxin A (ETA) carrying a deletion of glutamic acid-553, an important active-site residue, was expressed in an ETA-negative strain of P. aeruginosa and shown to be exported from the cells as efficiently as wild-type ETA. The mutant protein, purified from the culture medium, was devoid of ADP-ribosyltransferase activity. Protein conformation was barely perturbed by the deletion, as determined by a number of measures, including affinity for substrate NAD, proteinase sensitivity, absorbance and fluorescence spectroscopy, and differential scanning calorimetry. The conformational integrity and stability of the mutant toxin are consistent with potential use of the protein in vaccines or as a carrier in preparing conjugate vaccines.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Pseudomonas aeruginosa
/
Toxines bactériennes
/
Toxoïdes
/
ADP ribose transferases
/
Facteurs de virulence
/
Exotoxines
/
Glutamates
Langue:
En
Journal:
Biochim Biophys Acta
Année:
1992
Type de document:
Article