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Heat-labile toxin E. coli

Further studies concerning the activity of glycodendrons containing two or four peripheral GMjOS against the E. coli heat-labile toxin (LTBh) B-pentamer have been similarly described (Fig. 43).313... [Pg.293]

Cholera Toxin (CT) and E. coli Heat-Labile Toxin (LT)... [Pg.70]

The B subunit of the E. coli heat-labile toxin binds to the brush border of intestinal epithelial cells in a highly specific, lectinlike manner. Uptake of this toxin and transcytosis to the basolateral side of the enterocytes was observed both in vivo (63) and in vitro (64). [Pg.263]

Dallas, W. S., and Falkow, S., 1980, Amino acid sequence homology between cholera toxin and E. coli heat-labile toxin, Nature 288 499-201. [Pg.279]

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. [Pg.382]

Moravec, T., Schmidt, M.A., Herman, E.M., and Woodford-Thomas, T. (2007). Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine. Vaccine 25(9) 1647-1657. [Pg.54]

Beyer, A., Wang, K., Umble, A.N., Wolt, J.D., and Cunnick, J.E. (2007). Low-dose exposure and immunogenicity of transgenic maize expressing the Escherichia coli heat-labile toxin B subunit. Environ. Health Perspect. 115(3) 354-360. [Pg.171]

Gluck R, Mischler R, Durrer P, Furer E, Lang AB, Herzog C, Cryz SJ Jr. Safety and immunogenicity of intranasally administered inactivated trivalent virosome-formulated influenza vaccine containing Escherichia coli heat-labile toxin as a mucosal adjuvant J Infect Dis 2000 181(3) 1129-32. [Pg.1757]

Cholera toxin (CT) and E. coli heat-labile enterotoxin (LT-1 or LT) are members of the AB5 family of ADP-ribosylating toxins (Merritt and Hoi,... [Pg.18]

The mono(ADP-ribosyl)ation, the transfer of the ADP-ribose moiety of NAD to a macromolecule, was discovered by Hayaishi et al. in 1968 as the mechanism of the cytotoxic effect of diphtheria toxin [1], The substrate of this toxin-catalyzed ADP-ribosylation is elongation factor-2. The same reaction is catal)Azed by Pseudomonas toxin. The second bacterial toxin involved in mono(ADP-ribosyl)ation of mammalian cell proteins is cholera toxin, the substrate of which was identified as the guanine nucleotide-binding regulatory component of membrane adenylate cyclase in 1978 [2].E. coli heat-labile enterotoxin is similar to cholera toxin in many respects. [Pg.551]

The structure of E.coli heat-labile enterotoxin determined by X-ray crystallography and downloaded from the Protein Data Bank (see page 700). The protein has seven subunits—that is seven protein chains (Section 22.16). Five of them (blue, green purple, etc.) attach to a cell membrane. The toxin uses the red helical spike to deliver the catalytic subunit (orange) into the cell. The red and gray space-filling model is a protein side chain that acts as a base catalyst (Section 23.9). This toxin is responsible for what is known as traveler s diarrhea. [Pg.649]

Baldwin TJ, Knutton S, Sellers L, Hernandez HA, Aitken A, Williams PH Enteroaggregative Escherichia coli strains secrete a heat-labile toxin antigenically related to E. coli hemolysin. Infect Immun 1992,60 2092-2095. [Pg.33]

Enterotoxigenic E. coli B subunits of the heat labile toxin (LTB) Maize seed Elicited neutralizing antibodies. Immunogenic when administered orally. Serum and secretory immune responses in humans. Partially protective in mouse gut fluid assay. 27-29, 89, unpublished data... [Pg.144]

Enterotoxigenic E. coli are capable of producing two plasmid-mediated enterotoxins heat-labile toxin (HLT) and heat-stable toxin (HST)." A cholera-like toxin, HLT has two subunits (A and B) that... [Pg.2041]

The heat-labile toxin B subunit of E. coli (LTB) [398], hepatitis B surface antigen [404], respiratory syncytial virus F protein [258], measles virus hemagglutinin [180], and Norwalk virus capsid protein [240, 405, 406] have each been successfully expressed in plants and delivered orally in animals or humans to determine their im-munoprophylactic activity. The first account of a human clinical trial of oral vaccine based on an E. coli enterotoxin as... [Pg.868]

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. [Pg.389]

The heat-labile E. coli enterotoxin, whose gene is carried on a plasmid, is a close relative of cholera toxin11 0 and also catalyzes ADP ribosylation of arginine 201 of the Gsa subunit.111 Bordetella pertussis, which causes whooping cough, forms a similar toxin that attacks the inhibitory regulatory protein G v as well as transducin and inactivates them by ADP ribosylation. Diphtheria toxin (Box 29-A), the exotoxin from Pseudomonas aeruginosa, and the toxin from Clostridium botulinum also catalyze ADP-ribosylation reactions.k/1 ... [Pg.548]


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See also in sourсe #XX -- [ Pg.70 ]




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Heat-toxin

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