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Open data
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Basic information
Entry | Database: PDB / ID: 6igc | |||||||||||||||||||||
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Title | Crystal structure of HPV58/33/52 chimeric L1 pentamer | |||||||||||||||||||||
![]() | Major capsid protein L1 | |||||||||||||||||||||
![]() | STRUCTURAL PROTEIN / capsid protein | |||||||||||||||||||||
Function / homology | ![]() T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / host cell nucleus / virion attachment to host cell / structural molecule activity Similarity search - Function | |||||||||||||||||||||
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![]() | Li, Z.H. / Song, S. / He, M.Z. / Gu, Y. / Li, S.W. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Rational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity. Authors: Zhihai Li / Shuo Song / Maozhou He / Daning Wang / Jingjie Shi / Xinlin Liu / Yunbing Li / Xin Chi / Shuangping Wei / Yurou Yang / Zhiping Wang / Jinjin Li / Huilian Qian / Hai Yu / Qingbing ...Authors: Zhihai Li / Shuo Song / Maozhou He / Daning Wang / Jingjie Shi / Xinlin Liu / Yunbing Li / Xin Chi / Shuangping Wei / Yurou Yang / Zhiping Wang / Jinjin Li / Huilian Qian / Hai Yu / Qingbing Zheng / Xiaodong Yan / Qinjian Zhao / Jun Zhang / Ying Gu / Shaowei Li / Ningshao Xia / ![]() ![]() 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 ...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. | |||||||||||||||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 6.4 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 775.8 KB | Display | ![]() |
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Full document | ![]() | 890.7 KB | Display | |
Data in XML | ![]() | 501.3 KB | Display | |
Data in CIF | ![]() | 684.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9665C ![]() 9666C ![]() 9667C ![]() 6igdC ![]() 6igeC ![]() 6igfC ![]() 5y9eS S: Starting model for refinement C: citing same article ( |
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Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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