Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxin.

1996 ◽  
Vol 64 (12) ◽  
pp. 5413-5416 ◽  
Author(s):  
L de Haan ◽  
W R Verweij ◽  
I K Feil ◽  
T H Lijnema ◽  
W G Hol ◽  
...  
1979 ◽  
Vol 254 (14) ◽  
pp. 6270-6272 ◽  
Author(s):  
J Moss ◽  
S Garrison ◽  
N J Oppenheimer ◽  
S H Richardson

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.


1996 ◽  
Vol 271 (43) ◽  
pp. 27188
Author(s):  
Lloyd W. Ruddock ◽  
Jeremy J.F. Coen ◽  
Caroline Cheesman ◽  
Robert B. Freedman ◽  
Timothy R. Hirst

1999 ◽  
Vol 274 (13) ◽  
pp. 8764-8769
Author(s):  
Dubravka Matković-Calogović ◽  
Arianna Loregian ◽  
Maria Rosa D'Acunto ◽  
Roberto Battistutta ◽  
Alessandro Tossi ◽  
...  

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