We developed a rabbit polyclonal antiserum reactive against a recombinant 6x His-UL46 fusion protein expressed in* Escherichia coli , and using this antiserum identified the UL46 gene product of herpes simplex virus type 2 (HSV-2) to be phosphoproteins with apparent molecular masses of 82-, 84-, and 86-kDa in infected Vero cells. The UL46 protein was produced in the late phase of infection in a manner highly dependent on viral DNA synthesis, and was mainly distributed at the edge of the nucleus in the cytoplasm. Although its kinetics of production and its progress of distribution were different from those of the major tegument protein VP16 (the UL48 gene product or α-trans-inducing factor (αTIF)), most of the UL46 protein colocalized with VP16 in the late phase of infection, and copurified with it in column chromatography. Moreover, our data showed that the HSV-2 UL46 protein, when coexpressed with VP16, enhanced α4 promotor-regulated gene expression in a transient luciferase reporter assay, while the expression of the UL46 protein alone suppressed it.
Archives of Virology – Springer Journals
Published: Oct 1, 2000
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