Carlier D, Jean-Jean O, Fouillot N, Will H, Rossignol J M
Laboratoire de Génétique des Virus, UPR 2431-CNRS, Gif sur Yvette, France.
J Gen Virol. 1995 Apr;76 ( Pt 4):1041-5. doi: 10.1099/0022-1317-76-4-1041.
The hepatitis B virus (HBV) e antigen (HBeAg) is a 15 kDa soluble antigen derived from a precursor protein (precore protein) by two processing events, cleavage of the N-terminal signal peptide and cleavage of the C-terminal 34 amino acids. So far, the role of the C-terminal sequences in secretion has not been analysed in full. In this study deletion of the last 60 amino acids was found to abrogate HBeAg secretion whereas deletions of the last 10, 25 or 39 amino acids decreased its secretion rate. These data demonstrate that C-terminal precore protein sequences are crucial for HBe secretion and determine its secretion rate.
乙肝病毒(HBV)e抗原(HBeAg)是一种15 kDa的可溶性抗原,它由一种前体蛋白(前核心蛋白)经两个加工过程产生,即N端信号肽的切割和C端34个氨基酸的切割。到目前为止,C端序列在分泌过程中的作用尚未得到全面分析。在本研究中,发现缺失最后60个氨基酸会消除HBeAg的分泌,而缺失最后10、25或39个氨基酸则会降低其分泌率。这些数据表明,前核心蛋白的C端序列对HBe的分泌至关重要,并决定其分泌率。