ArticleThe Journal of biological chemistry2010
Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 113 citations in OpenAlex.
- Localization of the PelC and PelE effectors to theInfection and immunity · 2026Article
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- Subversion of the host endocytic pathway by Legionella pneumophila-mediated ubiquitination of Rab5.The Journal of cell biology · 2025Article
- ThemSphere · 2025Article
- In Vitro synergy of Farnesyltransferase inhibitors in combination with colistin against ESKAPE bacteria.PloS one · 2025Article
- Review
- Evaluating protein prenylation of human and viral CaaX sequences using a humanized yeast system.Disease models & mechanisms · 2024Article
- Monitoring host-pathogen interactions using chemical proteomics.RSC chemical biology · 2024Review
- A Humanized Yeast System for Evaluating the Protein Prenylation of a Wide Range of Human and Viral CaaX Sequences.bioRxiv : the preprint server for biology · 2023Article
- Brucella effectors NyxA and NyxB target SENP3 to modulate the subcellular localisation of nucleolar proteins.Nature communications · 2023Article
- Cellular cholesterol licensesMicrobial cell (Graz, Austria) · 2023Article
- ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions.Amino acids · 2022Article
- The Legionella pneumophila Effector RavY Contributes to a Replication-Permissive Vacuolar Environment during Infection.Infection and immunity · 2021Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Evolution and Adaptation ofBiomolecules · 2021Review
- Bacteria Are New Targets for Inhibitors of Human Farnesyltransferase.Frontiers in microbiology · 2021Article
- Review
- Structural insight into the membrane targeting domain of the Legionella deAMPylase SidD.PLoS pathogens · 2020Article
- Legionella pneumophila Excludes Autophagy Adaptors from the Ubiquitin-Labeled Vacuole in Which It Resides.Infection and immunity · 2020Article
- Divergent Evolution ofmBio · 2020Article
9 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The intracellular human pathogen Legionella pneumophila translocates multiple proteins in the host cytosol known as effectors, which subvert host cellular processes to create a membrane-bound organelle that supports bacterial replication. It was observed that several Legionella effectors encode a prototypical eukaryotic prenylation CAAX motif (where C represents a cysteine residue and A denotes an aliphatic amino acid). These bacterial motifs mediated posttranslational modification of effector proteins resulting in the addition of either a farnesyl or geranylgeranyl isoprenyl lipid moiety to the cysteine residue of the CAAX tetrapeptide. Lipidation enhanced membrane affinity for most Legionella CAAX motif proteins and facilitated the localization of these effector proteins to host organelles. Host farnesyltransferase and class I geranylgeranyltransferase were both involved in the lipidation of the Legionella CAAX motif proteins. Perturbation of the host prenylation machinery during infection adversely affected the remodeling of the Legionella-containing vacuole. Thus, these data indicate that Legionella utilize the host prenylation machinery to facilitate targeting of effector proteins to membrane-bound organelles during intracellular infection.
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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.