Shiga-like toxins

Suri Iyer et al. synthesized similar Gb3-AuNPs but with different length of linkers and surface glycan densities [66], They conducted luciferase assay to measure the toxin-mediated inhibition of protein synthesis and found that Gb3-AuNPs were nontoxic to Vero monkey kidney cells and protected Vero cells from Shiga toxin in a dose-dependent manner. 

FIGURE 16.8 Gb3 coated on (a) a carbohydrate core and (b) a gold nanoparticle used to study the binding interactions with Shiga-like toxin. 

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Samadapour M, J Liston, JE Ongerth, PI Tarr (1990) Evalnation of DNA probes for detection of Shiga-like-toxin-producing Escherichia coli in food and calf fecal samples. Appl Environ Microbiol 56 1212-1215. 

Tissue culture of susceptible mammalian cells may be used to characterize some bacteria by the toxins they produce. For example, Shiga-like toxins (verotoxins) are produced by E. coli 0157 H7.4,8... 

Low-iron stress in the host is a signal for pathogenic bacteria to induce virulence factors, such as Shiga-like toxin and haemolysins (although haemolysins could also help to obtain iron from lysed cells and could be grouped under iron uptake ). 

P. I. Kitov, J. M. Sadowska, G. Mulvey, G. D. Armstrong, H. Ling, N. Pannu, R. J. Read, and D. R. Bundle, Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands, Nature, 403 (2000) 669-672. 

Fig. 17. The STARFISH dodecamer of Kitov et al. with the Pk trisaccharide linked laterally at 2 and showing subnanomolar inhibitory activity against Shiga-like toxin I.23... 

Louise CB, Obrig TG Specific interaction of Escherichia coli 0157 H7-derived Shiga-like toxin II with human renal endothelial cells. J Infect Dis 1995 172 1397-1401. 

O Brien AD, Holmes RK Shiga and Shiga-like toxins. Microbiol Rev 1987 51 206-220. 

O Loughlin EV, Robins-Browne RM Effect of Shiga toxin and Shiga-like toxins on eukaryotic cells. Microbes Infect 2001 3 493-507. 

Donohue-Rolfe, Arthur, David W.K. Acheson, Anne V. Kane, and Gerald T. Keusch. "Purification of Shiga Toxin and Shiga-Like Toxins I and II by Receptor Analog Affinity Chromatography with Immobilized PI Glycoprotein and Production of Cross-Reactive Monoclonal Antibodies." Infection and Immunity 57 (December 1989) 3888-893. 

Huppertz, H. J., Busch, H., Schmidt, S., Aleksic, S., and Karch, H. (1996). Diarrhea in young children associated with Escherichia coli non-0157 organisms that produce Shiga-like toxin. /. Pediatr. 128, 341-346. 

C. botulinum toxins belong to the AB group of toxins, which also includes diphtheria toxin, pseudomonas exotoxin A, anthrax toxin, Shiga(like) toxin, cholera toxin, pertussis toxin, and plant toxins, e.g., ricin. Moiety A has an enzymatic activity and usually modified cellular-target entering cytosol. Moiety B consists of one or more components and binds the toxin to surface receptors, and is responsible for translocation of the A component into cells. AB toxins are produced in a non-active form and are activated by a split between two cysteine residues within a region (Falnes and Sandvig, 2000). 

CEGF-SLT comprises Cys-tagged EGF fused to catalytic subunit of E. coli Shiga-like toxin. 

Fig. 2.7.S. Potent decameric inhibitor of the shiga-like toxin from E. Coli [14].

St. Hilaire PM, Boyd MK, Toone EJ. Interaction of the Shiga-like toxin type 1 B-subunit with its carbohydrate receptor. Biochemistry 1994 33 14452-14463. 

Kitov PI, Sadowska JM, Mulvey G, Armstrong GD, Lingaw H, Pannu NS, Read RJ, Bundle DR. Shiga-like toxins are 193. 

Kitov PI, Shimizu H, Homans SW, Bundle DR. Optimization of tether length in nonglycosidically linked bivalent ligands that target sites 2 and 1 of a Shiga-like toxin. J. Am. Chem. Soc. 194. 2003 125 3284-3294. 

Kitov, P I, Bundle, D R, Synthesis and structure-activity relationships of di- and trisaccharide inhibitors for Shiga-like toxin type 1, J. Chem. Soc. Perkin. Trans., 1, 838-853, 2001. 

Potent decameric ligands for the AB5 toxin Shiga-like toxin... 

Several groups have employed polyamino acid backbones as templates for the display of multiple carbohydrate residues [164,165]. For example, potent E-selectin antagonists have been generated from poly lysine [166,167] These materials are highly effective inhibitors of leukocyte rolling. Multivalent polylysine displays have also been used to inhibit Shiga-like toxin binding [168]. 

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