Pääbo S, Weber F, Nilsson T, Schaffner W, Peterson P A
EMBO J. 1986 Aug;5(8):1921-7. doi: 10.1002/j.1460-2075.1986.tb04445.x.
The early transmembrane glycoprotein E19 of adenovirus-2 binds to class I antigens of the major histocompatibility complex (MHC). The association is initiated in the endoplasmic reticulum of infected cells and abrogates the intracellular transport of the class I molecules. To examine which parts of the E19 molecule are responsible for the association with the class I antigens and which parts confine the protein to the endoplasmic reticulum we have constructed a series of mutated E19 genes, which have been expressed in an improved mammalian expression vector. By various manipulations the membrane anchoring and the cytoplasmic domains were removed from the protein. The biosynthesis of the mutant protein was examined. All mutant proteins were secreted from the cells suggesting that the transmembrane and/or cytoplasmic portions of the E19 molecule are responsible for its confinement to the endoplasmic reticulum. The ability to associate with class I antigens was retained by the lumenal domain of the E19 protein.
腺病毒2型早期跨膜糖蛋白E19与主要组织相容性复合体（MHC）的I类抗原结合。这种结合在受感染细胞的内质网中开始，并废除了I类分子的细胞内转运。为了研究E19分子的哪些部分负责与I类抗原的结合，以及哪些部分将该蛋白限制在内质网中，我们构建了一系列突变的E19基因，这些基因已在一种改进的哺乳动物表达载体中表达。通过各种操作，从该蛋白中去除了膜锚定结构域和细胞质结构域。对突变蛋白的生物合成进行了检测。所有突变蛋白都从细胞中分泌出来，这表明E19分子的跨膜和/或细胞质部分负责将其限制在内质网中。E19蛋白的腔结构域保留了与I类抗原结合的能力。
