ArticleFrontiers in microbiology2011
Effector glycosyltransferases in legionella.
Article in Frontiers in microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Crystal structure of theVirulence · 2026Article
- Review
- Crystal structure of thebioRxiv : the preprint server for biology · 2025Article
- Glycosylating Effectors ofBiomolecules · 2022Review
- Glucosylation by the Legionella Effector SetA Promotes the Nuclear Localization of the Transcription Factor TFEB.iScience · 2020Article
- Characterization of the glucosyltransferase activity of Legionella pneumophila effector SetA.Naunyn-Schmiedeberg's archives of pharmacology · 2019Article
- The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins likeProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Post-translational modifications are key players of the Legionella pneumophila infection strategy.Frontiers in microbiology · 2015Review
- The transcriptome of Legionella pneumophila-infected human monocyte-derived macrophages.PloS one · 2014Article
- A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.Nature structural & molecular biology · 2013Article
- Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1.The Journal of biological chemistry · 2012Article
- Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis.PLoS pathogens · 2012Article
- Legionella: from protozoa to humans.Frontiers in microbiology · 2011Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legionella causes severe pneumonia in humans. The pathogen produces an array of effectors, which interfere with host cell functions. Among them are the glucosyltransferases Lgt1, Lgt2 and Lgt3 from L. pneumophila. Lgt1 and Lgt2 are produced predominately in the post-exponential phase of bacterial growth, while synthesis of Lgt3 is induced mainly in the lag-phase before intracellular replication of bacteria starts. Lgt glucosyltransferases are structurally similar to clostridial glucosylating toxins. The enzymes use UDP-glucose as a donor substrate and modify eukaryotic elongation factor eEF1A at serine-53. This modification results in inhibition of protein synthesis and death of target cells.In addition to Lgts, Legionella genomes disclose several genes, coding for effector proteins likely to possess glycosyltransferase activities, including SetA (subversion of eukaryotic vesicle trafficking A), which influences vesicular trafficking in the yeast model system and displays tropism for late endosomal/lysosomal compartments of mammalian cells. This review mainly discusses recent results on the structure-function relationship of Lgt glucosyltransferases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.