The US11 gene product of herpes simplex virus is an abundant virion structu
ral protein with RNA-binding regulatory activity. Its carboxyl-terminal hal
f consists of tandem tripeptide repeats of the sequence RXP. We demonstrate
that the US11 protein has intercellular trafficking activity and accumulat
es in the nucleolus when singly expressed in cultured cells, and that the R
XP repeats are responsible for this activity. These same properties were al
so observed in cells expressing a fusion protein linking US11 to the green
fluorescent protein. Furthermore, exogenous US11 protein was internalized b
y cells at 4 degreesC, which suggests that US11 protein uptake occurs prima
rily through an energy-independent pathway. (C) 2001 Academic Press.