Download Special Issue on Emerging Bacterial Toxins by Klaus Aktories, Ingo Just PDF

By Klaus Aktories, Ingo Just

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1998; Mahida et al. 1996, 1998; Qa’Dan et al. 2002). Apoptosis is induced by many signals, particularly by detachment of cells from their extracellular matrix (Ruoslahti 1997). The cytotoxins which are known to induce detachment through their actin filament-disrupting properties may induce apoptosis in the same way as EDTA or neutrophil elastase do (Shibata et al. 1996). Lethal toxin from C. sordellii was also reported to induce apoptosis in the myeloid cell line HL-60 through inactivation of Rac.

1998). Differences in substrate specificity are evident and based on the isoform of the toxin (see Table 1). , Thr-37 in RhoA and Thr-35 in Rac, Cdc42, Ras. a-toxin from C. novyi recruits UDP-N-acetyl-glucosamine (UDPglcNAc) and transfers the glcNAc to the same threonine residue in Rho, Rac, and Cdc42 as toxins A and B do (Selzer et al. 1996) (Table 1). The source of the transferred glucose is the ubiquitous nucleotide sugar UDP-glucose which is intracellularly present in micromolar range (Laughlin et al.

2003). Retention of configuration and the glucosyl transition state exclude a single SN2 reaction mechanism but rather argues for a binucleophilic substitution (double replacement) or a stereospecific SN1 reaction, where structural constraints of the catalytic pocket prevent formation of a racemate (Geyer et al. 2003; Vetter et al. 2000) Besides the UDP-glucose, a divalent cation is required to form a ternary complex between the enzyme (toxin), UDP-glucose and the metal ion; the ion is involved in nucleotide sugar binding.

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