Chimeric papillomavirus-like particles expressing a foreign epitope on capsid surface loops.
Chimeric papillomavirus-like particles expressing a foreign epitope on capsid surface loops.
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DOI：
10.1099/0022-1317-82-11-2799
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发表时间：
2001-11
期刊：
影响因子：
--
通讯作者：
Kirnbauer R
中科院分区：
文献类型：
--
作者：
Slupetzky K;Shafti-Keramat S;Lenz P;Brandt S;Grassauer A;Sara M;Kirnbauer R
中和衣壳表位是抗体介导的针对乳头瘤病毒（PV）感染和诱导疾病的免疫保护的重要决定因素。人PV-16型（HPV-16）和牛PV-1型（BPV-1）的L1主要衣壳蛋白与外源肽结合在几个衣壳表面环中自组装成五聚体或病毒样颗粒（VLP）的嵌合。中和单克隆抗体（MAb）的结合模式和小鼠免疫证实(i) aa 282-286和351-355附近的区域参与中和表位，并确定后者为免疫优势位点；（ii）将外源肽置于组装结构的背景下显着增强了其免疫原性。从野生型HPV-16和BPV-1 VLPs中拆卸的五聚体显示出一些在完全组装的VLPs上检测到的中和表位，但缺乏结合抑制细胞附着的中和单抗亚群。
Neutralization capsid epitopes are important determinants for antibody-mediated immune protection against papillomavirus (PV) infection and induced disease. Chimeric L1 major capsid proteins of the human PV type 16 (HPV-16) and the bovine PV type 1 (BPV-1) with a foreign peptide incorporated into several capsid surface loops self-assembled into pentamers or virus-like particles (VLP). Binding patterns of neutralizing monoclonal antibodies (MAb) and immunization of mice confirmed (i) that regions around aa 282–286 and 351–355 contribute to neutralization epitopes and identified the latter region as an immunodominant site and (ii) that placing a foreign peptide in the context of an assembled structure markedly enhanced its immunogenicity. Pentamers disassembled from wild-type HPV-16 and BPV-1 VLPs displayed some of the neutralization epitopes that were detected on fully assembled VLPs, but were deficient for binding a subset of neutralizing MAb that inhibit cell attachment.
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