Schmolke S, Tacke M, Schmitt U, Engel A M, Ofenloch-Haehnle B
Boehringer Mannheim GmbH, R&D Infectious Diseases, Penzberg, Germany.
J Virol. 1998 May;72(5):4541-5. doi: 10.1128/JVI.72.5.4541-4545.1998.
In order to elucidate the structure and morphology of hepatitis G virus (HGV), a recently isolated flavivirus, we generated a panel of eight monoclonal antibodies (MAbs) against the putative second envelope protein (E2) following DNA immunization. The MAbs were shown to be specific for four different epitopes on recombinant E2. MAb Mc6 was the only antibody able to detect the linear epitope LTGGFYEPL. In addition, Mc6 was able to immunoprecipitate viral particles in human blood samples as detected by reverse transcription-PCR amplification of HGV RNA. This precipitation could be competed by addition of saturating amounts of the linear peptide or abolished by addition of Nonidet P-40. We conclude that, albeit lacking the N-terminal sequence of a functional core protein, HGV builds classical viral particles displaying E2 envelope protein on their outer surfaces.
为了阐明最近分离出的黄病毒——庚型肝炎病毒（HGV）的结构和形态，我们在DNA免疫后制备了一组针对假定的第二包膜蛋白（E2）的八种单克隆抗体（MAb）。这些单克隆抗体被证明对重组E2上的四个不同表位具有特异性。单克隆抗体Mc6是唯一能够检测线性表位LTGGFYEPL的抗体。此外，Mc6能够免疫沉淀人血样本中的病毒颗粒，这可通过对HGV RNA进行逆转录-聚合酶链反应扩增来检测。加入饱和量的线性肽可竞争这种沉淀，加入非离子去污剂NP-40则可消除这种沉淀。我们得出结论，尽管HGV缺乏功能性核心蛋白的N端序列，但它仍能构建在其外表面展示E2包膜蛋白的经典病毒颗粒。
