Proteolytic processing of the hepatitis B virus e antigen precursor - Cleavage at two furin consensus sequences
Proteolytic processing of the hepatitis B virus e antigen precursor - Cleavage at two furin consensus sequences
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DOI：
10.1074/jbc.m207634200
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发表时间：
2003-01-10
影响因子：
4.8
通讯作者：
Rossignol, JM
中科院分区：
文献类型：
--
作者：
Messageot, F;Salhi, S;Rossignol, JM
B型肝炎病毒P22蛋白是一种非结构蛋白，是17-kDa分泌型e抗原（HBeAg）的前体。成熟的HBeAg是在去除P22的C-末端区域后获得的，这一过程涉及前蛋白转化酶。我们的研究表明，首先，蛋白酶可以在Arg（167）或Arg（154）的C-末端侧切割P22，其次，成熟过程可以在一个步骤或两个步骤中完成，并产生加工中间体（P20）。我们的数据还表明，P22 C末端的去除，这主要发生在trans-Golgi网络，也可以实现胞吐后。考虑到这一特征和切割位点的氨基酸序列，我们得出结论，弗林蛋白酶参与了HBeAg的成熟。此外，我们表明，在我们的实验系统中，HBeAg是一个164个氨基酸的蛋白质，而不是以前报道的159个氨基酸的蛋白质。
The Hepatitis B virus P22 protein is a nonstructural protein that is the precursor of the 17-kDa secreted e antigen (HBeAg). The mature HBeAg is obtained after the removal of the C-terminal region of P22, a process which involves a proprotein convertase. Our studies show first that the protease could cleave P22 at the C-terminal side of Arg(167) or Arg(154) and second, that the maturation process can be either done in one step or in two steps with the generation of a processing intermediate (P20). Our data also demonstrate that the removal of the P22 C terminus, which occurs mainly in the trans-Golgi network, can also be achieved after exocytosis. Keeping in mind this characteristic and the amino acid sequence of the cleavage sites, we concluded that furin is involved in the maturation of the HBeAg. In addition, we show that in our experimental system, the HBeAg is a 164-amino acid protein and not a 159-amino acid protein as previously reported.