LOCALIZATION AND PUTATIVE FUNCTION OF THE U(L)20 MEMBRANE-PROTEIN IN CELLS INFECTED WITH HERPES-SIMPLEX VIRUS-1

The U(L)20 protein of herpes simplex virus 1, an intrinsic membrane pr otein, is required in infected Vero cells in which the Golgi apparatus is fragmented for the transport of virions from the space between the inner and outer nuclear membranes and for the transport of fully proc essed cell membrane associated glycoproteins from the trans-Golgi to t he plasma membrane. It is not required in the human 143TK(-) cell line , in which the Golgi apparatus remains intact. We report the following . (i) The U(L)20 protein was detected in infected Cells beginning at 6 h postinfection and was regulated as a gamma(1) gene. (ii) Pulse chas e experiments revealed no detectable alteration in the mobility of the U(L)20 protein in polyacrylamide gels. (iii) In both infected Vero an d infected 143TK(-) cells, the U(L)20 protein was detected by immunofl uorescence in association with nuclear membranes and in the cytoplasm. Some of the cytoplasmic fluorescence colocalized with beta-COP, a pro tein associated with Golgi-derived transport vesicles. U(L)20 protein was present in virions purified from the extracellular space but could not be detected in the plasma membrane. These results are consistent with the hypothesis that U(L)20 is a component of virion envelopes and membranes of virion transport vesicles and is selectively retained fr om the latter in a Golgi compartment.