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TitleShigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 3099, Year 2025
Publish dateApr 1, 2025
AuthorsXindi Zhou / Huijing Zhang / Yaru Wang / Danni Wang / Zhiqiao Lin / Yuchao Zhang / Yubin Tang / Jianping Liu / Yu-Feng Yao / Yixiao Zhang / Lifeng Pan /
PubMed AbstractUbiquitination 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 ...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.
External linksNat Commun / PubMed:40164614 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.7 - 3.47 Å
Structure data

61848

9jw1

EMDB-61848, PDB-9jw1:
Cryo-EM structure of Human RNF213
Method: EM (single particle) / Resolution: 3.46 Å

61852

9jwg

EMDB-61852, PDB-9jwg:
Cryo-EM Focused Refined Map of Human RNF213 E3 module and IpaH1.4 LRR domain
Method: EM (single particle) / Resolution: 3.47 Å

PDB-9jta:
Crystal structure of RNF213 RING domain bound to IpaH1.4 LRR domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • shigella flexneri (bacteria)
  • shigella flexneri 5a str. m90t (bacteria)
KeywordsCYTOSOLIC PROTEIN / RNF213 / IpaH1.4

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