6CV1

CryoEM structure of human enterovirus D68 full particle (after incubation with heparin-derived hexasaccharide)

  • Classification: VIRUS
  • Organism(s): enterovirus D68
  • Mutation(s): No 

  • Deposited: 2018-03-27 Released: 2019-07-24 
  • Deposition Author(s): Liu, Y., Rossmann, M.G.
  • Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.76 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Bypassing pan-enterovirus host factor PLA2G16.

Baggen, J.Liu, Y.Lyoo, H.van Vliet, A.L.W.Wahedi, M.de Bruin, J.W.Roberts, R.W.Overduin, P.Meijer, A.Rossmann, M.G.Thibaut, H.J.van Kuppeveld, F.J.M.

(2019) Nat Commun 10: 3171-3171

  • DOI: https://doi.org/10.1038/s41467-019-11256-z
  • Primary Citation of Related Structures:  
    6CV1, 6CV2, 6CV3, 6CV4, 6CV5, 6CVB

  • PubMed Abstract: 

    Enteroviruses are a major cause of human disease. Adipose-specific phospholipase A2 (PLA2G16) was recently identified as a pan-enterovirus host factor and potential drug target. In this study, we identify a possible mechanism of PLA2G16 evasion by employing a dual glycan receptor-binding enterovirus D68 (EV-D68) strain. We previously showed that this strain does not strictly require the canonical EV-D68 receptor sialic acid. Here, we employ a haploid screen to identify sulfated glycosaminoglycans (sGAGs) as its second glycan receptor. Remarkably, engagement of sGAGs enables this virus to bypass PLA2G16. Using cryo-EM analysis, we reveal that, in contrast to sialic acid, sGAGs stimulate genome release from virions via structural changes that enlarge the putative openings for genome egress. Together, we describe an enterovirus that can bypass PLA2G16 and identify additional virion destabilization as a potential mechanism to circumvent PLA2G16.


  • Organizational Affiliation

    Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL, Utrecht, The Netherlands.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
viral protein 1297enterovirus D68Mutation(s): 0 
UniProt
Find proteins for A0A0X7Z9B1 (Human enterovirus D68)
Explore A0A0X7Z9B1 
Go to UniProtKB:  A0A0X7Z9B1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0X7Z9B1
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
viral protein 3247enterovirus D68Mutation(s): 0 
UniProt
Find proteins for E9RIT6 (Human enterovirus D68)
Explore E9RIT6 
Go to UniProtKB:  E9RIT6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupE9RIT6
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
viral protein 2248enterovirus D68Mutation(s): 0 
UniProt
Find proteins for A0A0X7Z9B1 (Human enterovirus D68)
Explore A0A0X7Z9B1 
Go to UniProtKB:  A0A0X7Z9B1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0X7Z9B1
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
viral protein 468enterovirus D68Mutation(s): 0 
UniProt
Find proteins for A0A0P0DH17 (Human enterovirus D68)
Explore A0A0P0DH17 
Go to UniProtKB:  A0A0P0DH17
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0P0DH17
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.76 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONjspr
MODEL REFINEMENTPHENIX
MODEL REFINEMENTREFMAC
MODEL REFINEMENTCoot

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)United StatesAI011219

Revision History  (Full details and data files)

  • Version 1.0: 2019-07-24
    Type: Initial release
  • Version 1.1: 2019-07-31
    Changes: Data collection, Database references
  • Version 1.2: 2019-12-18
    Changes: Author supporting evidence
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations