ArticleProceedings of the National Academy of Sciences of the United States of America2009
A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
106 citing papers in PubMed, 173 citations in OpenAlex.
- A functional screen for bacterial ubiquitin regulation identifies an unusual Pseudomonas aeruginosa E3 ligase.The EMBO journal · 2026Article
- The Manipulation of Host Cells byInternational journal of molecular sciences · 2026Review
- Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.Nature reviews. Immunology · 2026Review
- ThebioRxiv : the preprint server for biology · 2026Article
- Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2.RSC chemical biology · 2026Article
- Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213.Nature structural & molecular biology · 2025Article
- Review
- The Type III Effector NopM from Bradyrhizobium elkanii USDA61 Induces a Hypersensitive Response in Lotus japonicus Root Nodules.Microbes and environments · 2025Article
- TheBiochemistry · 2024Article
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Article
- The Attenuation Mechanism and Live Vaccine Potential of a Low-VirulenceJournal of microbiology and biotechnology · 2023Article
- Insights into the GSDMB-mediated cellular lysis and its targeting by IpaH7.8.Nature communications · 2023Article
- The emerging role and therapeutic implications of bacterial and parasitic deubiquitinating enzymes.Frontiers in immunology · 2023Review
- Subversion of GBP-mediated host defense by E3 ligases acquired during Yersinia pestis evolution.Nature communications · 2022Article
- Role of an FNIP Repeat Domain-Containing Protein Encoded by Megavirus Baoshan during Viral Infection.Journal of virology · 2022Article
- The NEL Family of Bacterial E3 Ubiquitin Ligases.International journal of molecular sciences · 2022Review
- Different epitopes of Ralstonia solanacearum effector RipAW are recognized by two Nicotiana species and trigger immune responses.Molecular plant pathology · 2022Article
- Discovery and characterization of a new genotype ofFrontiers in microbiology · 2022Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Processes as diverse as receptor binding and signaling, cytoskeletal dynamics, and programmed cell death are manipulated by mimics of host proteins encoded by pathogenic bacteria. We show here that the Salmonella virulence factor SspH2 belongs to a growing class of bacterial effector proteins that harness and subvert the eukaryotic ubiquitination pathway. This virulence protein possesses ubiquitination activity that depends on a conserved cysteine residue. A crystal structure of SspH2 reveals a canonical leucine-rich repeat (LRR) domain that interacts with a unique E3 ligase [which we have termed NEL for Novel E3 Ligase] C-terminal fold unrelated to previously observed HECT or RING-finger E3 ligases. Moreover, the LRR domain sequesters the catalytic cysteine residue contained in the NEL domain, and we suggest a mechanism for activation of the ligase requiring a substantial conformational change to release the catalytic domain for function. We also show that the N-terminal domain targets SspH2 to the apical plasma membrane of polarized epithelial cells and propose a model whereby binding of the LRR to proteins at the target site releases the ligase domain for site-specific function.
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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.