Menotti L, Mirandola P, Locati M, Campadelli-Fiume G
Section on Microbiology and Virology, Department of Experimental Pathology, University of Bologna, Bologna, Italy.
J Virol. 1999 Jan;73(1):325-33. doi: 10.1128/JVI.73.1.325-333.1999.
The sequence of human herpesvirus 6 (HHV-6) U51 open reading frame predicts a protein of 301 amino acid residues with seven transmembrane domains. To identify and characterize U51, we derived antipeptide polyclonal antibodies and developed a transient expression assay. We ascertained that U51 was synthesized in cord blood mononuclear cells infected with either variant A- or variant B-HHV-6 and was transported to the surface of productively infected cells. When synthesized in transient expression systems, U51 intracellular trafficking was regulated in a cell-type-dependent fashion. In human monolayer HEK-293 and 143tk- cells, U51 accumulated predominantly in the endoplasmic reticulum and failed to be transported to the cell surface. In contrast, in T-lymphocytic cell lines J-Jhan, Molt-3, and Jurkat, U51 was successfully transported to the plasma membrane. We infer that transport of U51 to the cell surface requires a cell-specific function present in activated T lymphocytes and T-cell lines.
人类疱疹病毒6型（HHV - 6）U51开放阅读框的序列预测其编码的蛋白含有301个氨基酸残基，并具有七个跨膜结构域。为了鉴定和表征U51，我们制备了抗肽多克隆抗体并开发了瞬时表达检测方法。我们确定U51在感染A变体或B变体HHV - 6的脐血单个核细胞中合成，并被转运到高效感染细胞的表面。当在瞬时表达系统中合成时，U51的细胞内运输以细胞类型依赖的方式受到调控。在人单层HEK - 293和143tk - 细胞中，U51主要在内质网中积累，无法转运到细胞表面。相比之下，在T淋巴细胞系J - Jhan、Molt - 3和Jurkat中，U51成功转运到质膜。我们推断，U51转运到细胞表面需要活化T淋巴细胞和T细胞系中存在的细胞特异性功能。
