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- W168934269 abstract "Legionella is a gram-negative bacterium and the causative pathogen of legionellosis—a severe pneumonia in humans. A large number of Legionella effectors interfere with numerous host cell functions, including intracellular vacuole trafficking and maturation, phospholipid metabolism, protein ubiquitination, pro-/anti-apoptotic balances or inflammatory responses. Moreover, eukaryotic protein synthesis is affected by L. pneumophila glucosyltransferases Lgt1, Lgt2, and Lgt3. Structurally, these enzymes are similar to large clostridial cytotoxins, use UDP-glucose as a co-substrate and modify a conserved serine residue (Ser-53) in elongation factor 1A (eEF1A). The ternary complex consisting of eEF1A, GTP, and aminoacylated-tRNA seems to be the substrate for Lgts. Studies with Saccharomyces cerevisiae corroborated that eEF1A is the major target responsible for Lgt-induced cytotoxic activity. In addition to Lgt proteins, Legionella produces other effector glycosyltransferase, including the modularly composed protein SetA, which displays tropism for early endosomal compartments, subverts host cell vesicle trafficking and demonstrates toxic activities toward yeast and mammalian cells. Here, our current knowledge about both groups of L. pneumophila glycosylating effectors is reviewed." @default.
- W168934269 created "2016-06-24" @default.
- W168934269 creator A5066655987 @default.
- W168934269 creator A5072111511 @default.
- W168934269 creator A5080600755 @default.
- W168934269 date "2013-01-01" @default.
- W168934269 modified "2023-10-16" @default.
- W168934269 title "Cytotoxic Glucosyltransferases of Legionella pneumophila" @default.
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- W168934269 doi "https://doi.org/10.1007/82_2013_338" @default.
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