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TitleRational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 5360, Year 2018
Publish dateDec 18, 2018
AuthorsZhihai 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 /
PubMed AbstractSequence 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.
External linksNat Commun / PubMed:30560935 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.5 - 12.3 Å
Structure data

EMDB-9665:
The cryoEM map of HPV33 VLP in complex with the Fab fragment of antibody 4E5
Method: EM (single particle) / Resolution: 12.3 Å

EMDB-9666:
The cryoEM map of HPV58/33 chimeric VLP in complex with the Fab fragment of antibody 4E5
Method: EM (single particle) / Resolution: 12.0 Å

EMDB-9667:
The cryoEM map of HPV58/33/52 chimeric VLP in complex with the Fab fragment of antibody 4E5
Method: EM (single particle) / Resolution: 10.0 Å

PDB-6igc:
Crystal structure of HPV58/33/52 chimeric L1 pentamer
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-6igd:
Crystal structure of HPV58/33 chimeric L1 pentamer
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6ige:
Crystal structure of Human Papillomavirus type 33 pentamer
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-6igf:
Crystal structure of Human Papillomavirus type 52 pentamer
Method: X-RAY DIFFRACTION / Resolution: 2.751 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • human papillomavirus type 58
  • human papillomavirus type 33
  • human papillomavirus type 52
KeywordsSTRUCTURAL PROTEIN / capsid protein / Human Papillomavirus type 52 capsid protein

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