Background: Legionella pneumophila glucosyltransferase Lgt1 modifies elongation factor 1A and Hbs1 (Hsp70 subfamily B suppressor 1). Results: In Saccharomyces cerevisiae deleted of endogenous eEF1A and Hbs1, Lgt1 inhibits growth by glucosylation of ectopically expressed eEF1A at serine 53. Conclusion: Glucosylation of eEF1A but not of Hbs1 is essential for Lgt1-induced toxicity. Significance: Yeast as a model to study the action of Legionella glucosyltransferases.
Aggregatibacter actinomycetemcomitans is a gram negative bacterium and an infectious agent of human diseases with severe oral and extra oral manifestations. One of the major virulence factors in this microorganism is cytolethal distending toxin (CDT). This toxin consists of three subunits-A, B, and C and is able to disrupt cell cycle by intrinsic DNAse activity of its B-subunit. Due to the fact that this protein can represent an important component of diagnostic, prophylactic and therapeutic preparations, production of CDT subunits in preparative quantities is of considerable practical importance. In the current study we demonstrated that deletion of NH 2 -terminal regions from the molecules of CDT-A, -B, or -C resulted in 20-400-fold increase in production of the corresponding subunits. These truncated molecules were used as immunogens to raise monospecific sera, which were shown in western blot to react specifically with the homologous subunits of cytolethal distending toxin.
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