Delpeyroux F, Chenciner N, Lim A, Malpièce Y, Blondel B, Crainic R, van der Werf S, Streeck R E
Science. 1986 Jul 25;233(4762):472-5. doi: 10.1126/science.2425433.
The hepatitis B virus (HBV) envelope protein carrying the surface antigen (HBsAg) is assembled with cellular lipids in mammalian cells into empty viral envelopes. In a study to evaluate the capacity of such particles to present foreign peptide sequences in a biologically active form, in-phase insertions were created in the S gene encoding the major envelope protein. One of the sequences inserted was a synthetic DNA fragment encoding a poliovirus neutralization epitope. Mammalian cells expressing the modified gene secreted hybrid particles closely resembling authentic 22-nanometer HBsAg particles. These particles reacted with a poliovirus-specific monoclonal antibody and induced neutralizing antibodies against poliovirus. The results indicate that empty viral envelopes of HBV may provide a means for the presentation of peptide sequences and for their export from mammalian cells.
携带表面抗原(HBsAg)的乙型肝炎病毒(HBV)包膜蛋白在哺乳动物细胞中与细胞脂质组装成空的病毒包膜。在一项评估此类颗粒以生物活性形式呈递外源肽序列能力的研究中,在编码主要包膜蛋白的S基因中产生了同相插入。插入的序列之一是编码脊髓灰质炎病毒中和表位的合成DNA片段。表达修饰基因的哺乳动物细胞分泌出与正宗的22纳米HBsAg颗粒非常相似的杂交颗粒。这些颗粒与脊髓灰质炎病毒特异性单克隆抗体发生反应,并诱导产生针对脊髓灰质炎病毒的中和抗体。结果表明,HBV的空病毒包膜可能为肽序列的呈递及其从哺乳动物细胞中的输出提供一种手段。