ArticlePLoS pathogens2010
NleG Type 3 effectors from enterohaemorrhagic Escherichia coli are U-Box E3 ubiquitin ligases.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 93 citations in OpenAlex.
- Design of a live-attenuated bacterial vaccine using effector network engineering.Nature communications · 2026Article
- Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.Nature reviews. Immunology · 2026Review
- Identification and characterization of a ubiquitin E3 RING ligase of the Chlamydia-like bacterium Simkania negevensis.PLoS pathogens · 2025Article
- Article
- Escherichia coli HPI-induced duodenitis through ubiquitin regulation of the TLR4/NF-κB pathway.BMC veterinary research · 2025Article
- ThemSphere · 2025Article
- Identification of a genomic cluster related to hypersecretion of intestinal mucus and mucinolytic activity of atypical enteropathogenicFrontiers in cellular and infection microbiology · 2024Article
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- UBE2E2 enhances Snail-mediated epithelial-mesenchymal transition and Nrf2-mediated antioxidant activity in ovarian cancer.Cell death & disease · 2023Article
- Distinct Molecular Features of NleG Type 3 Secreted Effectors Allow for Different Roles during Citrobacter rodentium Infection in Mice.Infection and immunity · 2023Article
- Conservation lost: host-pathogen battles drive diversification and expansion of gene families.The FEBS journal · 2021Review
- TcpC inhibits toll-like receptor signaling pathway by serving as an E3 ubiquitin ligase that promotes degradation of myeloid differentiation factor 88.PLoS pathogens · 2021Article
- Bacterial nucleomodulins: A coevolutionary adaptation to the eukaryotic command center.PLoS pathogens · 2021Review
- Modification of the host ubiquitome by bacterial enzymes.Microbiological research · 2020Review
- The bacterial deubiquitinase Ceg23 regulates the association of Lys-63-linked polyubiquitin molecules on theThe Journal of biological chemistry · 2020Article
- TheLife science alliance · 2019Article
- Ubiquitination-Mediated Inflammasome Activation during Bacterial Infection.International journal of molecular sciences · 2019Review
- Prediction of bacterial E3 ubiquitin ligase effectors using reduced amino acid peptide fingerprinting.PeerJ · 2019Article
- Revisiting Bacterial Ubiquitin Ligase Effectors: Weapons for Host Exploitation.International journal of molecular sciences · 2018Review
- Ubiquitin, SUMO, and NEDD8: Key Targets of Bacterial Pathogens.Trends in cell biology · 2018Review
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
NleG homologues constitute the largest family of Type 3 effectors delivered by pathogenic E. coli, with fourteen members in the enterohaemorrhagic (EHEC) O157:H7 strain alone. Identified recently as part of the non-LEE-encoded (Nle) effector set, this family remained uncharacterised and shared no sequence homology to other proteins including those of known function. The C-terminal domain of NleG2-3 (residues 90 to 191) is the most conserved region in NleG proteins and was solved by NMR. Structural analysis of this structure revealed the presence of a RING finger/U-box motif. Functional assays demonstrated that NleG2-3 as well as NleG5-1, NleG6-2 and NleG9' family members exhibited a strong autoubiquitination activity in vitro; a characteristic usually expressed by eukaryotic ubiquitin E3 ligases. When screened for activity against a panel of 30 human E2 enzymes, the NleG2-3 and NleG5-1 homologues showed an identical profile with only UBE2E2, UBE2E3 and UBE2D2 enzymes supporting NleG activity. Fluorescence polarization analysis yielded a binding affinity constant of 56+/-2 microM for the UBE2D2/NleG5-1 interaction, a value comparable with previous studies on E2/E3 affinities. The UBE2D2 interaction interface on NleG2-3 defined by NMR chemical shift perturbation and mutagenesis was shown to be generally similar to that characterised for human RING finger ubiquitin ligases. The alanine substitutions of UBE2D2 residues Arg5 and Lys63, critical for activation of eukaryotic E3 ligases, also significantly decreased both NleG binding and autoubiquitination activity. These results demonstrate that bacteria-encoded NleG effectors are E3 ubiquitin ligases analogous to RING finger and U-box enzymes in eukaryotes.
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