Heat-labile enterotoxin

Bacterial toxins Heat-labile enterotoxin of Ecoli and cholera toxin... 

Spangler B.D., Wilkinson E.A., Murphyb J.T., Tyler B.J., Comparison of the Spreeta surface plasmon resonance sensor and a quartz crystal microbalance for detection of Escherichia coli heat-labile enterotoxins, Analytica Chimica Acta 2001 444 149-161. 

FIG. 30. The best ligands against E. coli heat-labile enterotoxin. 

J. C. Pickens, E. A. Merritt, M. Ahn, C. L. M. J. Verlinde, W. G. J. Hoi, and E. Fan, Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes, Chem. Biol., 9 (2002) 215-224. 

J. P. Thompson and C.-L. Schengrund, Oligosaccharide-derivatized dendrimers Defined multivalent inhibitors of the adherence of the cholera toxin B subunit and the heat labile enterotoxin of E. coli to GM1, Glycoconjug. J., 14 (1997) 837-845. 

Navarro-Garcia F, Eslava C, Villaseca JM, Lo-pez-Revilla R, Czeczulin JR, Srinivas S, Nataro JP, Cravioto A In vitro effects of a high-molecular-weight heat-labile enterotoxin from enteroaggregative Escherichia coli. Infect Immun 1998,66 3149-3154. 

E. coli B subunit of the heat labile enterotoxin (LTB) fused to an immu-nocontraceptive epitope Tomato fruit and leaves No immunogenicity assays performed. 91... 

B. D. Spangler,E. A. Wilkinson, J. T. Murphy, and B. J. Tyler, "Comparison of the Spreeta Surface plasmon Resonance Sensor and a Quartz Crystal Microbalance for Detection of Escherichia Coh heat-labile Enterotoxin," Analytica Chimica Acta 444, 149-161 (2001). 

Chikwamba R, Cunnick J, Hathaway D, McMurray J, Mason H, Wang K. (2002) A functional antigen in a practical crop LT-B producing maize protects mice against Escherichia coli heat labile enterotoxin (LT) and cholera toxin (CT). Transgenic Res 11 479 93. 

There are a large number of proteins that share this designation. Perhaps the best known is the heat-labile enterotoxin from E. coli that catalyzes the ADP-ribosyla-tion of a number of proteins. 

Cholera toxin (CT) and heat-labile enterotoxin (LT) cause gastroenteric disorders such as stomach ache and diarrhea 8), The toxins consist of one A subunit and five B... 

The most potent mucosal adjuvants have been shown to be the toxins derived from Vibrio cholerae or Escherichia coli, which should not be surprising since these organisms invade the body through the GI tract. Obviously too toxic for human use because they are the source of cholera or diarrhoea, heat labile enterotoxins have been tested in mice and shown to be potent adjuvants for orally or nasally administered influenza vaccine. The potency of heat-labile enterotoxin mutants may also be enhanced by formulation into bioadhesive particulate delivery systems, and this is an area under current exploration. 

Minke, W. E., Diller, D. J., Hoi, W. G. J., and Verlinde, C. (1999) The role of waters in docking strategies with incremental flexibility for carbohydrate derivatives heat-labile enterotoxin, a multivalent test case. J. Med. Chem. 42,1778-1788. 

Mineral Salts Immunostimulatory adjuvants Lipid particles Particulate adjuvants Mucosal adjuvants Aluminium hydroxide, aluminium phosphate, calcium phosphate Saponins (e.g., QS21), MDP derivatives, bacterial DNA (CpG oligos), LPS, MPL and synthetic derivatives, lipopeptides, cytokines (e.g., GM-CSF, IL-2, IL-12) Liposomes, virosomes, iscoms, cochleates, emulsions (e.g., Freunds adjuvant, SAF, MF59 ) Poloxamer particles, virus-like particles, PLG microparticles Cholera toxin (CT), mutant toxin (e.g., LTK63, LTR72), heat labile enterotoxin (LT), microparticles, polymerized liposomes, chitosan... 

Ryan, E.T. Crean, T.I. John, M. Butterton, J.R. Clements, J.D. Calderwood, S.B. Vivo expression and immunoadjuvancy of a mutant of heat-labile enterotoxin of escherichia coli in vaccine and vector strains of vibrio cholerae. Infect. Immun. 1999, 67, 1694—1701. 

Cholera toxin and the very similar (in structure and mechanism of action) heat-labile enterotoxin from E. coli (LT-1 or LT, which is responsible for the syndrome of traveler s diarrhea) have been widely applied as molecular tools to facilitate understanding of signalling systems. Examples of molecules besides Gs that were identified because of work on CT are the ADP-ribosylation factors (ARFs), now known to play a critical role in intracellular vesicular transport (Moss and Vaughan, 1995), and the mammalian ADP-ribosyltransferases (Zolkiewska et al., 1994). As more is learned about CT structure and biochemistry, modified or mutant CT and LT molecules are being gen-... 

Merritt EA, Pronk SE, Sixmo TK, et al. (1994a) Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 A resolution. In FEBS Let. 337 88-92. 

Merritt EA, Sarfaty S, Pizza M, et al. (1995) Mutation of a buried residue causes loss of activity, but no conformational change in the heat-labile enterotoxin of Escherichia coli. In Struct. Biol. 2 269-272. 

Moss J, Garrison S, Oppenheimer NJ, et al. (1979b) NAD-dependent ADP-ribosylation of arginine and proteins by Escherichia coli heat-labile enterotoxin. In J. Biol. Chem. 254 6270-6272. 

Moss J, Vaughan M, (1988a) Mechanism of action of choleragen (cholera toxin) and coli heat-labile enterotoxins. In Bacterial Toxins (Handbook of Natural Toxins), 4, (Tu AT, Hardegree MC) Dekker, New York. 

Sixmo TK, Kalk KH, van Zanten BAM, et al. (1993) Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. In J. Mo/. Biol. 230 890-918. 

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