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首页> 外文期刊>Molecular and Cellular Biology >Hepatitis B surface antigen: an unusual secreted protein initially synthesized as a transmembrane polypeptide.
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Hepatitis B surface antigen: an unusual secreted protein initially synthesized as a transmembrane polypeptide.

机译：乙型肝炎表面抗原：一种不寻常的分泌蛋白，最初合成为跨膜多肽。

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摘要

Hepatitis B surface antigen (HBsAg), the major coat protein of hepatitis B virus, is also secreted from cells as a subviral particle, without concomitant cleavage of N-terminal amino acid sequences. We examined this unusual export process in a cell-free system and showed that the initial product of HBsAg biosynthesis is an integral transmembrane protein, with most or all of its C-terminal half on the lumenal side of the endoplasmic reticulum membrane. To study the nature of its topogenic signals, we synthesized fusion proteins between HBsAg and the nonsecreted protein alpha-globin. Fusion proteins in which approximately 100 amino acids of globin preceded all HBsAg sequences were successfully translocated in vitro; the same domain as in the wild-type HBsAg was transported into the vesicle lumen. Fusions in which the entire globin domain was C terminal were able to translocate both the C-terminal region of HBsAg and its attached globin domain. Thus, uncleaved signal sequences in p24s function to direct portions of the molecule across the membrane and are able to perform this function even when positioned in an internal protein domain.
机译：乙型肝炎表面抗原（HBsAg）是乙型肝炎病毒的主要外壳蛋白，也作为亚病毒颗粒从细胞中分泌出来，而不会伴随N端氨基酸序列的裂解。我们在无细胞系统中检查了这种异常的输出过程，结果表明HBsAg生物合成的初始产物是必不可少的跨膜蛋白，其大部分或全部C端一半位于内质网腔侧。为了研究其拓扑信号的性质，我们合成了HBsAg和非分泌蛋白α-珠蛋白之间的融合蛋白。在所有HBsAg序列之前，珠蛋白的大约100个氨基酸融合蛋白已在体外成功转移;与野生型HBsAg相同的结构域被转运至囊泡内腔。整个球蛋白结构域为C端的融合体能够转移HBsAg的C端区域及其附着的球蛋白结构域。因此，p24s中未切割的信号序列的功能是引导分子的一部分穿过膜，即使位于内部蛋白质结构域中也能够执行此功能。

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