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- PDB-7ffo: Cryo-EM structure of VEEV VLP at the 5-fold axes -

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Basic information

Entry
Database: PDB / ID: 7ffo
TitleCryo-EM structure of VEEV VLP at the 5-fold axes
Components
  • Capsid proteinCapsid
  • Spike glycoprotein E1
  • Spike glycoprotein E2
  • assembly protein E3
KeywordsVIRUS LIKE PARTICLE / Virus / Receptor / Complex
Function / homology
Function and homology information


togavirin / T=4 icosahedral viral capsid / suppression by virus of host gene expression / clathrin-dependent endocytosis of virus by host cell / virion attachment to host cell / fusion of virus membrane with host endosome membrane / host cell cytoplasm / viral envelope / host cell nucleus / serine-type endopeptidase activity ...togavirin / T=4 icosahedral viral capsid / suppression by virus of host gene expression / clathrin-dependent endocytosis of virus by host cell / virion attachment to host cell / fusion of virus membrane with host endosome membrane / host cell cytoplasm / viral envelope / host cell nucleus / serine-type endopeptidase activity / host cell plasma membrane / virion membrane / structural molecule activity / RNA binding / integral component of membrane
Similarity search - Function
Peptidase S3, togavirin / Alphavirus core protein (CP) domain profile. / Alphavirus E1 glycoprotein / Alphavirus E3 glycoprotein / Alphavirus core protein / Alphavirus E2 glycoprotein / Alphavirus E2 glycoprotein, domain C / Alphavirus E2 glycoprotein, domain B / Alphavirus E2 glycoprotein, domain A / Alphavirus E1 glycoprotein ...Peptidase S3, togavirin / Alphavirus core protein (CP) domain profile. / Alphavirus E1 glycoprotein / Alphavirus E3 glycoprotein / Alphavirus core protein / Alphavirus E2 glycoprotein / Alphavirus E2 glycoprotein, domain C / Alphavirus E2 glycoprotein, domain B / Alphavirus E2 glycoprotein, domain A / Alphavirus E1 glycoprotein / Alphavirus E3 spike glycoprotein / Alphavirus E2 glycoprotein / Flaviviral glycoprotein E, dimerisation domain / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Immunoglobulin E-set / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Structural polyprotein
Similarity search - Component
Biological speciesVenezuelan equine encephalitis virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsZhang, X. / Xiang, Y. / Ma, J. / Ma, B. / Huang, C.
CitationJournal: Nature / Year: 2021
Title: Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3.
Authors: Bingting Ma / Cuiqing Huang / Jun Ma / Ye Xiang / Xinzheng Zhang /
Abstract: 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 ...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.
History
DepositionJul 23, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 20, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 17, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID

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Assembly

Deposited unit
K: Capsid protein
L: assembly protein E3
N: Spike glycoprotein E2
O: Spike glycoprotein E1


Theoretical massNumber of molelcules
Total (without water)132,5354
Polymers132,5354
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Capsid protein / Capsid / Coat protein / C


Mass: 30980.801 Da / Num. of mol.: 1 / Mutation: K64N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Venezuelan equine encephalitis virus (strain TC-83)
Strain: TC-83 / Production host: Homo sapiens (human) / References: UniProt: P05674, togavirin
#2: Protein assembly protein E3 / p130


Mass: 6488.601 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Venezuelan equine encephalitis virus (strain TC-83)
Strain: TC-83 / Production host: Homo sapiens (human) / References: UniProt: P05674
#3: Protein Spike glycoprotein E2 / p62 / pE2


Mass: 47113.746 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Venezuelan equine encephalitis virus (strain TC-83)
Strain: TC-83 / Production host: Homo sapiens (human) / References: UniProt: P05674
#4: Protein Spike glycoprotein E1 / E1 envelope glycoprotein


Mass: 47952.066 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Venezuelan equine encephalitis virus (strain TC-83)
Strain: TC-83 / Production host: Homo sapiens (human) / References: UniProt: P05674

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Venezuelan equine encephalitis virus (strain TC-83) / Type: VIRUS / Entity ID: #1-#4 / Source: RECOMBINANT
Source (natural)Organism: Venezuelan equine encephalitis virus (strain TC-83)
Source (recombinant)Organism: Homo sapiens (human)
Details of virusEmpty: YES / Enveloped: YES / Isolate: STRAIN / Type: VIRUS-LIKE PARTICLE
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 344824 / Symmetry type: POINT

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