8UA4
Structure of eastern equine encephalitis virus VLP in complex with VLDLR LA1
Summary for 8UA4
| Entry DOI | 10.2210/pdb8ua4/pdb |
| EMDB information | 42050 |
| Descriptor | Envelope glycoprotein E1, Envelope glycoprotein E2, Capsid protein, ... (7 entities in total) |
| Functional Keywords | alphaviruses, receptor, virus like particle |
| Biological source | Eastern equine encephalitis virus More |
| Total number of polymer chains | 17 |
| Total formula weight | 532427.77 |
| Authors | Abraham, J.,Yang, P.,Li, W.,Fan, X.,Pan, J. (deposition date: 2023-09-20, release date: 2024-08-14, Last modification date: 2025-06-04) |
| Primary citation | Yang, P.,Li, W.,Fan, X.,Pan, J.,Mann, C.J.,Varnum, H.,Clark, L.E.,Clark, S.A.,Coscia, A.,Basu, H.,Smith, K.N.,Brusic, V.,Abraham, J. Structural basis for VLDLR recognition by eastern equine encephalitis virus. Nat Commun, 15:6548-6548, 2024 Cited by PubMed Abstract: Eastern equine encephalitis virus (EEEV) is the most virulent alphavirus that infects humans, and many survivors develop neurological sequelae, including paralysis and intellectual disability. Alphavirus spike proteins comprise trimers of heterodimers of glycoproteins E2 and E1 that mediate binding to cellular receptors and fusion of virus and host cell membranes during entry. We recently identified very-low density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) as cellular receptors for EEEV and a distantly related alphavirus, Semliki Forest virus (SFV). Here, we use single-particle cryo-electron microscopy (cryo-EM) to determine structures of the EEEV and SFV spike glycoproteins bound to the VLDLR ligand-binding domain and found that EEEV and SFV interact with the same cellular receptor through divergent binding modes. Our studies suggest that the ability of LDLR-related proteins to interact with viral spike proteins through very small footprints with flexible binding modes results in a low evolutionary barrier to the acquisition of LDLR-related proteins as cellular receptors for diverse sets of viruses. PubMed: 39095394DOI: 10.1038/s41467-024-50887-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.58 Å) |
Structure validation
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