Open AccessThe Herpes Simplex Virus 1 U L 34 Protein Interacts with a Cytoplasmic Dynein Intermediate Chain and Targets Nuclear Membrane
Author(s) -
GuoJie Ye,
Kevin T. Vaughan,
Richard B. Vallee,
Bernard Roizman
Publication year - 2000
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.74.3.1355-1363.2000
Subject(s) - biology , capsid , viral tegument , herpes simplex virus , nuclear membrane , microbiology and biotechnology , phosphoprotein , viral protein , nuclear transport , nuclear pore , nuclear protein , dynein , viral structural protein , transport protein , vesicle associated membrane protein 8 , cell nucleus , cytoplasm , virus , viral entry , viral replication , virology , membrane protein , phosphorylation , biochemistry , membrane , gene , microtubule , transcription factor
To express the function encoded in its genome, the herpes simplex virus 1 capsid-tegument structure released by deenvelopment during entry into cells must be transported retrograde to the nuclear pore where viral DNA is released into the nucleus. This path is essential in the case of virus entering axons of dorsal root ganglia. The objective of the study was to identify the viral proteins that may be involved in the transport. We report the following findings. (i) The neuronal isoform of the intermediate chain (IC-1a) of the dynein complex pulled down, from lysates of [35 S]methionine-labeled infected cells, two viral proteins identified as the products of UL 34 and UL 31 open reading frames, respectively. UL 34 protein is a virion protein associated with cellular membranes and phosphorylated by the viral kinase US 3. UL 31 protein is a largely insoluble, evenly dispersed nuclear phosphoprotein required for optimal processing and packaging of viral DNA into preformed capsids. Reciprocal pulldown experiments verified the interaction of IC-1a and UL 34 protein. In similar experiments, UL 34 protein was found to interact with UL 31 protein and the major capsid protein ICP5. (ii) To determine whether UL 34 protein is transported to the nuclear membrane, a requirement if it is involved in transport, the UL 34 protein was inserted into a baculovirus vector under the cytomegalovirus major early promoter. Cells infected with the recombinant baculovirus expressed UL 34 protein in a dose-dependent manner, and the UL 34 protein localized primarily in the nuclear membrane. An unexpected finding was that UL 34-expressing cells showed a dissociation of the inner and outer nuclear membranes reminiscent of the morphologic changes seen in cells productively infected with herpes simplex virus 1. UL 34, like many other viral proteins, may have multiple functions expressed both early and late in infection.