PROTEINS SPECIFIED BY HERPES SIMPLEX VIRUS .I. TIME OF SYNTHESIS TRANSFER INTO NUCLEI AND PROPERTIES OF PROTEINS MADE IN PRODUCTIVELY INFECTED CELLS

Polyacrylamide gel electrophoresis revealed at least 25 proteins synthesized at one time or another during productive infection of HEp-2 cells with herpes simplex virus. The proteins were made in the cytoplasm. The transfer of proteins from cytoplasm into the nucleus was slow and selective; less than half of the proteins synthesized during a short pulse appeared in the nucleus after a 3-hour chase. Moreover, proteins in 3 bands appeared to be restricted to the cytoplasm. Most of the proteins chased into the nucleus late in infection were identified on the basis of electrophoretic mobility as being structural viral proteins. All but a few proteins made late in infection could be chased into naked and enveloped nucleocapsids. The size of herpes virus proteins, estimated by co-electrophoresis with poliovirus proteins of known molecular weight, range to about 125,000 daltons. © 1968.