Standring D N, Ou J H, Rutter W J
Proc Natl Acad Sci U S A. 1986 Dec;83(24):9338-42. doi: 10.1073/pnas.83.24.9338.
Infection with hepatitis B virus (HBV) is associated with the production of a viral envelope particle that contains membrane lipids, surface antigen (S), and two presurface-antigens (pre-S) comprised of the entire S moiety with approximately 55 (pre-S2) and 174 (pre-S1) additional NH2-terminal amino acids. We show here that Xenopus oocytes injected with synthetic S mRNA assemble and secrete characteristic 22-nm viral envelope particles. In contrast, pre-S1 and pre-S2 antigens are synthesized but not secreted. By coinjecting mRNAs, we found that synthesis of high levels of pre-S proteins specifically inhibits S antigen secretion. On the other hand, high levels of S synthesis can drive the secretion of small amounts of either pre-S antigen. These observations are consistent with a model for viral envelope assembly in which both S and pre-S proteins are incorporated into a multimeric particle, presumably via interactions between the S protein domains, while the pre-S amino-terminal moieties regulate the secretion of this structure. Our results indicate that Xenopus oocytes will provide a powerful system for studying the morphogenesis of simple structures of viral or cellular origin.
感染乙肝病毒（HBV）与一种病毒包膜颗粒的产生有关，该颗粒包含膜脂、表面抗原（S）以及两种前表面抗原（pre-S），其中pre-S由整个S部分以及额外的约55个（pre-S2）和174个（pre-S1）氨基末端氨基酸组成。我们在此表明，注射了合成S mRNA的非洲爪蟾卵母细胞组装并分泌特征性的22纳米病毒包膜颗粒。相比之下，pre-S1和pre-S2抗原虽能合成但不会分泌。通过共注射mRNA，我们发现高水平pre-S蛋白的合成会特异性抑制S抗原的分泌。另一方面，高水平的S合成能驱动少量任一pre-S抗原的分泌。这些观察结果与病毒包膜组装模型一致，即S蛋白和pre-S蛋白都通过S蛋白结构域之间的相互作用被整合到多聚体颗粒中，而pre-S氨基末端部分调节该结构的分泌。我们的结果表明，非洲爪蟾卵母细胞将为研究病毒或细胞来源的简单结构的形态发生提供一个强大的系统。
