The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment.
The UL34 gene of herpes simplex virus type 2 (HSV-2) is highly conserved in the herpesvirus family. The UL34 gene product was identified In lysates of HSV-2-infected cells as protein species with molecular masses of 31 and 32.5 kDa, the latter being a phosphorylated product. Synthesis of these proteins occurred at late times post-infection and was highly dependent on viral DNA synthesis. Immunofluorescence assays revealed that the UL34 protein was localized in the cytoplasm in a continuous net-like structure, closely resembling the staining pattern of the endoplasmic reticulum (ER), in both HSV-2-infected cells and in cells transiently expressing UL34 protein. Deletion mutant analysis showed that this colocalization required the C terminus of the UL34 protein. The UL34 protein associated with virions but not with A, B or C capsids. We treated virions, HSV-2-infected cells and cells expressing the UL34 protein with a protease in order to examine the topology of the UL34 protein. In addition, we constructed UL34 deletion mutant proteins and examined their intracellular localization. Our data strongly support the hypothesis that the UL34 protein is inserted into the viral envelope as a tail-anchored type II membrane protein and is significant for virus envelopment.
Shiba
C
C
Department of Applied Biological Science, Science University of Tokyo, Faculty of Science & Technology, 2641 Yamazaki, Noda 278-8510, Japan2.|Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
Daikoku
T
T
Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
Goshima
F
F
Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
Takakuwa
H
H
Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
Yamauchi
Y
Y
Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
Koiwai
O
O
Department of Applied Biological Science, Science University of Tokyo, Faculty of Science & Technology, 2641 Yamazaki, Noda 278-8510, Japan2.
Nishiyama
Y
Y
Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan1.
D000818:Animals; D000918:Antibody Specificity; D002213:Capsid / Q000378:metabolism; D002522:Chlorocebus aethiops; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis; D019084:Fluorescent Antibody Technique, Indirect; D018258:Herpesvirus 2, Human / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed; D021281:Quantitative Structure-Activity Relationship; D011817:Rabbits; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000096:biosynthesis; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D014771:Virion / Q000378:metabolism
D004279:DNA, Viral; D008565:Membrane Proteins; C403420:UL34 protein, Human herpesvirus 1; D014759:Viral Envelope Proteins; D014764:Viral Proteins