ArticleNature communications2025
Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Intracranial Arterial Stenosis beyond Atherosclerosis: Insights from RNF213.Journal of atherosclerosis and thrombosis · 2026Review
- RNF213-dependent lytic destruction ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Listeria promotes systemic infection by targeting the host deubiquitinase CYLD.Nature communications · 2026Article
- Mechanisms and strategies of host xenophagy manipulation by intracellular bacteria.Cellular and molecular life sciences : CMLS · 2026Review
- Review
- An Rnf213-deficient hypoperfusion model reveals Moyamoya-relevant neurovascular remodeling.Angiogenesis · 2026Article
- Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria.Current opinion in microbiology · 2026Review
- Profiling Selectivity for theBiochemistry · 2026Article
- TheeLife · 2025Article
- HoweLife · 2025Article
- Genomic insights into Shigella species isolated from small ruminants and manure in the North West Province, South Africa.Applied microbiology and biotechnology · 2025Article
- The multifaceted role of RNF213 in oncogenesis: current insights and future research directions.Discover oncology · 2025Review
- ThebioRxiv : the preprint server for biology · 2025Article
- Proximity biotinylation at the host-bioRxiv : the preprint server for biology · 2025Article
- Host SUMOylation in bacterial infections and immune defense mechanisms.Frontiers in microbiology · 2025Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Ubiquitination plays vital roles in modulating pathogen-host cell interactions. RNF213, a E3 ligase, can catalyze the ubiquitination of lipopolysaccharide (LPS) and is crucial for antibacterial immunity in mammals. Shigella flexneri, an LPS-containing pathogenic bacterium, has developed mechanisms to evade host antibacterial defenses during infection. However, the precise strategies by which S. flexneri circumvents RNF213-mediated antibacterial immunity remain poorly understood. Here, through comprehensive biochemical, structural and cellular analyses, we reveal that the E3 effector IpaH1.4 of S. flexneri can directly target human RNF213 via a specific interaction between the IpaH1.4 LRR domain and the RING domain of RNF213, and mediate the ubiquitination and proteasomal degradation of RNF213 in cells. Furthermore, we determine the cryo-EM structure of human RNF213 and the crystal structure of the IpaH1.4 LRR/RNF213 RING complex, elucidating the molecular mechanism underlying the specific recognition of RNF213 by IpaH1.4. Finally, our cell based functional assays demonstrate that the targeting of host RNF213 by IpaH1.4 promotes S. flexneri proliferation within infected cells. In summary, our work uncovers an unprecedented strategy employed by S. flexneri to subvert the key host immune factor RNF213, thereby facilitating bacterial proliferation during invasion.
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