8IHP

Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3

This is a non-PDB format compatible entry.

Summary for 8IHP

• Entry DOI: 10.2210/pdb8ihp/pdb
• EMDB information: 35451
• Descriptor: Spike glycoprotein E2, Spike glycoprotein E1, Capsid protein, ... (6 entities in total)
• Functional Keywords: semliki forest virus, sfv, receptor, complex, vldlr, glycoprotein, viral protein
• Biological source: Semliki Forest virus (SFV); More
• Total number of polymer chains: 15
• Total formula weight: 464693.35

Authors

Cao, D.,Ma, B.,Cao, Z.,Zhang, X.,Xiang, Y. (deposition date: 2023-02-23, release date: 2023-04-12, Last modification date: 2025-07-02)

Primary citation

Cao, D.,Ma, B.,Cao, Z.,Zhang, X.,Xiang, Y.
Structure of Semliki Forest virus in complex with its receptor VLDLR.
Cell, 186:2208-2218.e15, 2023

PubMed Abstract: Semliki Forest virus (SFV) is an alphavirus that uses the very-low-density lipoprotein receptor (VLDLR) as a receptor during infection of its vertebrate hosts and insect vectors. Herein, we used cryoelectron microscopy to study the structure of SFV in complex with VLDLR. We found that VLDLR binds multiple E1-DIII sites of SFV through its membrane-distal LDLR class A (LA) repeats. Among the LA repeats of the VLDLR, LA3 has the best binding affinity to SFV. The high-resolution structure shows that LA3 binds SFV E1-DIII through a small surface area of 378 Å, with the main interactions at the interface involving salt bridges. Compared with the binding of single LA3s, consecutive LA repeats around LA3 promote synergistic binding to SFV, during which the LAs undergo a rotation, allowing simultaneous key interactions at multiple E1-DIII sites on the virion and enabling the binding of VLDLRs from divergent host species to SFV.

PubMed: 37098345
DOI: 10.1016/j.cell.2023.03.032

Experimental method

ELECTRON MICROSCOPY (3 Å)