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. 1986 Aug;5(8):1921–1927. doi: 10.1002/j.1460-2075.1986.tb04445.x

Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein.

S Pääbo, F Weber, T Nilsson, W Schaffner, P A Peterson
PMCID: PMC1167059  PMID: 3019670

Abstract

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.

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