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TitleThe receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 6866, Year 2024
Publish dateAug 10, 2024
AuthorsDuanfang Cao / Bingting Ma / Ziyi Cao / Xiaoyu Xu / Xinzheng Zhang / Ye Xiang /
PubMed AbstractEastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of ...Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of EEEV. Herein, we performed cryo-electron microscopy structural and biochemistry studies on the specific interactions between EEEV and VLDLR. Our results show that VLDLR binds EEEV at three different sites A, B and C through its membrane-distal LDLR class A (LA) repeats. Site A is located in the cleft in between the E1-E2 heterodimers. Site B is located near the connecting β ribbon of E2 and is in proximity to site A, while site C is on the domain B of E2. The binding of VLDLR LAs to EEEV is in complex modes, including the LA1-2 and LA3-5 mediated two major modes. Disruption of the LA1-2 mediated binding significantly affect the cell attachment of EEEV. However, the mutation W132G of VLDLR impairs the binding of LA3, drives the switch of the binding modes, and significantly enhances the attachment of EEEV to the cell. The W132G variant of VLDLR could be identified in human genome and SNP sequences, implying that people with similar mutations in VLDLR may be highly susceptible to EEEV infection.
External linksNat Commun / PubMed:39127734 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 11.0 Å
Structure data

38370

8xi4

EMDB-38370, PDB-8xi4:
Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-2
Method: EM (single particle) / Resolution: 3.4 Å

38371

8xi5

EMDB-38371, PDB-8xi5:
Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA3-5
Method: EM (single particle) / Resolution: 3.4 Å

38376

8ys2

EMDB-38376: Overall structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-2
PDB-8ys2: Overall structure of Eastern Equine Encephalitis virus VLP in complex with the receptor VLDLR LA1-2
Method: EM (single particle) / Resolution: 5.2 Å

38377

8ys4

EMDB-38377: Overall structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA3-5
PDB-8ys4: Overall structure of Eastern Equine Encephalitis virus VLP in complex with the receptor VLDLR LA3-5
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-38378: Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-8
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-38379: Structure of Eastern Equine Encephalitis VLP incubated with ApoER2 isoform2 LA1-3 (no receptor binding)
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-38380: Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-3
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-38381: Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA2-3
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-38382: Structure of Eastern Equine Encephalitis VLP in complex with the receptor VLDLR LA1-6-W132A
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-38383: Structure of Eastern Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-38384: Structure of Eastern Equine Encephalitis VLP PE6-K206E in complex with the receptor VLDLR LA1-8
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • eastern equine encephalitis virus
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / East Equine Encephalitis virus / EEEV / receptor / complex / VLDLR / glycoprotein / VIRUS LIKE PARTICLE / Eastern Equine Encephalitis virus / alphavirus

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