Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxin.
The Escherichia coli heat-labile enterotoxin (LT) is a potent inducer of mucosal immune responses. In a previous study (L. DeHaan, W. R. Verweij, M. Holtrop, E. Agsteribbe, and J. Wilschut, Vaccine 14:620-626, 1996), we have shown that efficient induction of an LTB-specific mucosal immune response by LT requires the presence of the LTA chain, suggesting a possible role of the enzymatic activity of LTA in the induction of these responses. In the present study, we generated LT mutants with altered ADP-ribosylation activities and evaluated their immunogenicity upon intranasal administration to mice. The results demonstrate that the mucosal immunogenicity of LT is not dependent on its ADP-ribosylation activity.
de Haan
L
L
Department of Physiological Chemistry, Groningen Institute for Drug Studies, University of Groningen, The Netherlands.
Verweij
W R
WR
Feil
I K
IK
Lijnema
T H
TH
Hol
W G
WG
Agsteribbe
E
E
Wilschut
J
J
D000244:Adenosine Diphosphate / Q000235:genetics / Q000276:immunology; D000818:Animals; D004768:Enterotoxins / Q000235:genetics* / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics* / Q000276:immunology; D006358:Hot Temperature; D018928:Immunity, Mucosal; D051379:Mice; D009154:Mutation
D004768:Enterotoxins; D000244:Adenosine Diphosphate