Fleury M J J, Touzé A, Alvarez E, Carpentier G, Clavel C, Vautherot J-F, Coursaget P
INSERM U618, Université François Rabelais, Tours, France.
Arch Virol. 2006 Aug;151(8):1511-23. doi: 10.1007/s00705-006-0734-y. Epub 2006 Mar 3.
The majority of the neutralizing epitopes of papillomaviruses (PV) are conformation-specific and have not been fully characterised. Studies have, to date, been limited to a few HPV types only. We analysed the epitopes on the major capsid protein (L1) of Human papillomavirus (HPV) type 31 using monoclonal antibodies (MAbs) generated against HPV-31 virus-like particles (VLPs). The type-specific MAbs against HPV-31 were all found to be neutralizing and recognized conformation-dependent epitopes. Two other MAbs directed against a conformational epitope were found to be cross-reactive with other HPV types, and one of them was found to be cross-neutralizing. Cross-reactive antibodies were further investigated using wild-type HPV-16 L1 VLPs and two mutants. The results obtained suggested the existence of a cross-neutralizing conformational epitope at the N-terminal part of the FG loop of the major capsid protein, and the other four cross-reactive MAbs recognized epitopes also located at the N-terminal part of the FG loop.
乳头瘤病毒(PV)的大多数中和表位具有构象特异性,尚未得到充分表征。迄今为止,研究仅局限于少数几种人乳头瘤病毒(HPV)类型。我们使用针对人乳头瘤病毒31型(HPV-31)病毒样颗粒(VLP)产生的单克隆抗体(MAb),分析了HPV-31主要衣壳蛋白(L1)上的表位。所有针对HPV-31的型特异性MAb均具有中和作用,并识别构象依赖性表位。另外两种针对构象表位的MAb被发现与其他HPV类型具有交叉反应性,其中一种具有交叉中和作用。使用野生型HPV-16 L1 VLP和两种突变体对交叉反应性抗体进行了进一步研究。所得结果表明,在主要衣壳蛋白FG环的N端部分存在一个交叉中和性构象表位,其他四种交叉反应性MAb识别的表位也位于FG环的N端部分。