6IGD

Crystal structure of HPV58/33 chimeric L1 pentamer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Rational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity.

Li, Z.Song, S.He, M.Wang, D.Shi, J.Liu, X.Li, Y.Chi, X.Wei, S.Yang, Y.Wang, Z.Li, J.Qian, H.Yu, H.Zheng, Q.Yan, X.Zhao, Q.Zhang, J.Gu, Y.Li, S.Xia, N.

(2018) Nat Commun 9: 5360-5360

  • DOI: https://doi.org/10.1038/s41467-018-07199-6
  • Primary Citation of Related Structures:  
    6IGC, 6IGD, 6IGE, 6IGF

  • PubMed Abstract: 

    Sequence variability in surface-antigenic sites of pathogenic proteins is an important obstacle in vaccine development. Over 200 distinct genomic sequences have been identified for human papillomavirus (HPV), of which more than 18 are associated with cervical cancer. Here, based on the high structural similarity of L1 surface loops within a group of phylogenetically close HPV types, we design a triple-type chimera of HPV33/58/52 using loop swapping. The chimeric VLPs elicit neutralization titers comparable with a mix of the three wild-type VLPs both in mice and non-human primates. This engineered region of the chimeric protein recapitulates the conformational contours of the antigenic surfaces of the parental-type proteins, offering a basis for this high immunity. Our stratagem is equally successful in developing other triplet-type chimeras (HPV16/35/31, HPV56/66/53, HPV39/68/70, HPV18/45/59), paving the way for the development of an improved HPV prophylactic vaccine against all carcinogenic HPV strains. This technique may also be extrapolated to other microbes.


  • Organizational Affiliation

    State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, Xiamen University, Xiamen, China, 361102.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major capsid protein L1
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
524human papillomavirus 58Mutation(s): 6 
Gene Names: L1
UniProt
Find proteins for P26535 (Human papillomavirus 58)
Explore P26535 
Go to UniProtKB:  P26535
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26535
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 153.686α = 90
b = 105.833β = 99.55
c = 154.713γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of ChinaChina81701637
National Science Foundation (China)China81701637
National Natural Science Foundation of ChinaChinaU1705283
National Science Foundation (China)ChinaU1705283
National Natural Science Foundation of ChinaChina31670935
National Science Foundation (China)China31670935

Revision History  (Full details and data files)

  • Version 1.0: 2018-11-21
    Type: Initial release
  • Version 1.1: 2019-01-02
    Changes: Data collection, Database references
  • Version 1.2: 2023-11-22
    Changes: Data collection, Database references, Refinement description