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Structure paper

TitleStructure of Venezuelan equine encephalitis virus with its receptor LDLRAD3.
Journal, issue, pagesNature, Vol. 598, Issue 7882, Page 677-681, Year 2021
Publish dateOct 13, 2021
AuthorsBingting Ma / Cuiqing Huang / Jun Ma / Ye Xiang / Xinzheng Zhang /
PubMed AbstractVenezuelan equine encephalitis virus (VEEV) is an enveloped RNA virus that causes encephalitis and potentially mortality in infected humans and equines. At present, no vaccines or drugs are available ...Venezuelan equine encephalitis virus (VEEV) is an enveloped RNA virus that causes encephalitis and potentially mortality in infected humans and equines. At present, no vaccines or drugs are available that prevent or cure diseases caused by VEEV. Low-density lipoprotein receptor class A domain-containing 3 (LDLRAD3) was recently identified as a receptor for the entry of VEEV into host cells. Here we present the cryo-electron microscopy structure of the LDLRAD3 extracellular domain 1 (LDLRAD3-D1) in complex with VEEV virus-like particles at a resolution of 3.0 Å. LDLRAD3-D1 has a cork-like structure and is inserted into clefts formed between adjacent VEEV E2-E1 heterodimers in the viral-surface trimer spikes through hydrophobic and polar contacts. Mutagenesis studies of LDLRAD3-D1 identified residues that are involved in the key interactions with VEEV. Of note, some of the LDLRAD3-D1 mutants showed a significantly increased binding affinity for VEEV, suggesting that LDLRAD3-D1 may serve as a potential scaffold for the development of inhibitors of VEEV entry. Our structures provide insights into alphavirus assembly and the binding of receptors to alphaviruses, which may guide the development of therapeutic countermeasures against alphaviruses.
External linksNature / PubMed:34646021
MethodsEM (single particle)
Resolution3.0 - 3.5 Å
Structure data

31566

7ffe

EMDB-31566, PDB-7ffe:
Cryo-EM structure of VEEV VLP
Method: EM (single particle) / Resolution: 3.5 Å

31567

7fff

EMDB-31567, PDB-7fff:
Structure of Venezuelan equine encephalitis virus with the receptor LDLRAD3
Method: EM (single particle) / Resolution: 3.0 Å

31568

7ffl

EMDB-31568, PDB-7ffl:
Cryo-EM structure of VEEV VLP-LDLRAD3-D1 complex at the 2-fold axes
Method: EM (single particle) / Resolution: 3.1 Å

31569

7ffn

EMDB-31569, PDB-7ffn:
Cryo-EM structure of VEEV VLP-LDLRAD3-D1 complex at the 5-fold axes
Method: EM (single particle) / Resolution: 3.0 Å

31570

7ffo

EMDB-31570, PDB-7ffo:
Cryo-EM structure of VEEV VLP at the 5-fold axes
Method: EM (single particle) / Resolution: 3.5 Å

31571

7ffq

EMDB-31571, PDB-7ffq:
Cryo-EM structure of VEEV VLP at the 2-fold axes
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • venezuelan equine encephalitis virus (strain tc-83)
  • homo sapiens (human)
KeywordsVIRUS LIKE PARTICLE / Virus / Receptor / Complex / VIRUS LIKE PARTICLE/PROTEIN BINDING / VIRUS LIKE PARTICLE-PROTEIN BINDING complex

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