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6IGF

Crystal structure of Human Papillomavirus type 52 pentamer

Summary for 6IGF
Entry DOI10.2210/pdb6igf/pdb
DescriptorMajor capsid protein L1 (1 entity in total)
Functional Keywordshuman papillomavirus type 52 capsid protein, structural protein
Biological sourceHuman papillomavirus type 52
Total number of polymer chains10
Total formula weight595336.76
Authors
Li, Z.H.,Song, S.,He, M.Z.,Gu, Y.,Li, S.W. (deposition date: 2018-09-25, release date: 2018-11-28, Last modification date: 2023-11-22)
Primary citationLi, 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.
Rational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity.
Nat Commun, 9:5360-5360, 2018
Cited by
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.
PubMed: 30560935
DOI: 10.1038/s41467-018-07199-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.751 Å)
Structure validation

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