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6IGC

Crystal structure of HPV58/33/52 chimeric L1 pentamer

これはPDB形式変換不可エントリーです。
6IGC の概要
エントリーDOI10.2210/pdb6igc/pdb
分子名称Major capsid protein L1 (1 entity in total)
機能のキーワードcapsid protein, structural protein
由来する生物種Human papillomavirus type 58
タンパク質・核酸の鎖数40
化学式量合計2365772.04
構造登録者
Li, Z.H.,Song, S.,He, M.Z.,Gu, Y.,Li, S.W. (登録日: 2018-09-25, 公開日: 2018-11-21, 最終更新日: 2023-11-22)
主引用文献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.
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.5 Å)
構造検証レポート
Validation report summary of 6igc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-18に公開中

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