Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis

Biochemistry ◽  
1993 ◽  
Vol 32 (49) ◽  
pp. 13566-13574 ◽  
Author(s):  
Masahiro Iwakura ◽  
Bryan E. Jones ◽  
Christopher J. Falzone ◽  
C. Robert Matthews
Biochemistry ◽  
1991 ◽  
Vol 30 (46) ◽  
pp. 11092-11103 ◽  
Author(s):  
Mark S. Warren ◽  
Katherine A. Brown ◽  
Martin F. Farnum ◽  
Elizabeth E. Howell ◽  
Joseph Kraut

Biochemistry ◽  
1987 ◽  
Vol 26 (13) ◽  
pp. 4093-4100 ◽  
Author(s):  
Jin Tann Chen ◽  
Kazunari Taira ◽  
Chen Pei D. Tu ◽  
Stephen J. Benkovic

1992 ◽  
Vol 267 (32) ◽  
pp. 22830-22836 ◽  
Author(s):  
K Ostanin ◽  
E.H. Harms ◽  
P.E. Stevis ◽  
R Kuciel ◽  
M.M. Zhou ◽  
...  

1994 ◽  
Vol 180 (6) ◽  
pp. 2147-2153 ◽  
Author(s):  
M Pizza ◽  
M R Fontana ◽  
M M Giuliani ◽  
M Domenighini ◽  
C Magagnoli ◽  
...  

Escherichia coli enterotoxin (LT) and the homologous cholera toxin (CT) are A-B toxins that cause travelers' diarrhea and cholera, respectively. So far, experimental live and killed vaccines against these diseases have been developed using only the nontoxic B portion of these toxins. The enzymatically active A subunit has not been used because it is responsible for the toxicity and it is reported to induce a negligible titer of toxin neutralizing antibodies. We used site-directed mutagenesis to inactivate the ADP-ribosyltransferase activity of the A subunit and obtained nontoxic derivatives of LT that elicited a good titer of neutralizing antibodies recognizing the A subunit. These LT mutants and equivalent mutants of CT may be used to improve live and killed vaccines against cholera and enterotoxinogenic E. coli.


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