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TitleMolecular basis of ApoER2-mediated Semliki Forest virus entry.
Journal, issue, pagesNat Commun, Year 2025
Publish dateDec 19, 2025
AuthorsBingchen Du / Xiyong Song / Bingyu Zhao / Zhibin Shi / Zaisi Liu / Shida Wang / Lili Wei / Xijun He / Juha T Huiskonen / Decheng Yang / Jingfei Wang /
PubMed AbstractThe very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) serve as entry receptors for the Semliki Forest virus (SFV). VLDLR interacts with the SFV E1 domain III ...The very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) serve as entry receptors for the Semliki Forest virus (SFV). VLDLR interacts with the SFV E1 domain III (DIII) through multiple LDLR class A (LA) domains. However, the ApoER2-mediated SFV entry mechanism remains unclear. Here, we perform biochemical and cellular results and determine the cryogenic electron microscopy (cryo-EM) structures of SFV complexed with ApoER2 LA5 and full-length ApoER2, demonstrating that among the seven LA domains of ApoER2 isoform 1, only LA5 specifically binds to the SFV E1-DIII via a limited interface (353 Ų) and facilitates cell attachment and entry. Site-directed mutagenesis confirms the significance of the residues at the SFV-ApoER2 interface. Significantly, a soluble LA5 decoy receptor neutralizes SFV infection and protects mice from lethal SFV challenge. These findings reveal a LA5-dependent receptor engagement mechanism for SFV entry via ApoER2, distinct from VLDLR.
External linksNat Commun / PubMed:41419770
MethodsEM (single particle)
Resolution2.7 - 4.2 Å
Structure data

EMDB-53901: Icosahedral reconstruction of Semliki Forest virus in complex with ApoER2 LA5
Method: EM (single particle) / Resolution: 3.6 Å

53902

9rbq

EMDB-53902, PDB-9rbq:
Semliki Forest virus trimer 1 in complex with ApoER2 LA5
Method: EM (single particle) / Resolution: 2.7 Å

53903

9rbr

EMDB-53903, PDB-9rbr:
Semliki Forest virus trimer 2 in complex with ApoER2 LA5
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-53904: Composite density map of Semliki Forest virus in complex with ApoER2 LA5
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-53905: Icosahedral reconstruction of Semliki Forest virus in complex with ApoER2 ligand-binding domain
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-53906: Semliki Forest virus trimer 1 in complex with ApoER2 ligand-binding domain
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-53907: Semliki Forest virus trimer 2 in complex with ApoER2 ligand-binding domain
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-53908: Composite density map of Semliki Forest virus in complex with ApoER2 ligand-binding domain
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • semliki forest virus
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsVIRUS / Semliki Forest virus / SFV / ApoER2 receptor / localized reconstruction

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