Intracellular Traffic of Herpes Simplex Virus Glycoprotein gE: Characterization of the Sorting Signals Required for Its trans -Golgi Network Localization
Autor: | Bernard Hoflack, Beate Sodeik, Ulrike Bauer, Agustin Alconada |
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Rok vydání: | 1999 |
Předmět: |
viruses
Molecular Sequence Data Immunology Golgi Apparatus Biology Transfection medicine.disease_cause Microbiology Virus Conserved sequence symbols.namesake Viral Envelope Proteins Virology medicine Animals Humans Simplexvirus Inner membrane Amino Acid Sequence Conserved Sequence chemistry.chemical_classification virus diseases Biological Transport Golgi apparatus Molecular biology Virus-Cell Interactions Herpes simplex virus chemistry Cytoplasm Insect Science symbols Rabbits Glycoprotein Intracellular HeLa Cells |
Zdroj: | Journal of Virology. 73:377-387 |
ISSN: | 1098-5514 0022-538X |
Popis: | Herpes simplex virus (HSV) and varicella-zoster virus (VZV) are two pathogenic human alphaherpesviruses whose intracellular assembly is thought to follow different pathways. VZV presumably acquires its envelope in the trans -Golgi network (TGN), and it has recently been shown that its major envelope glycoprotein, VZV-gE, accumulates in this compartment when expressed alone. In contrast, the envelopment of HSV has been proposed to occur at the inner nuclear membrane, although to which compartment the gE homolog (HSV-gE) is transported is unknown. For this reason, we have studied the intracellular traffic of HSV-gE and have found that this glycoprotein accumulates at steady state in the TGN, both when expressed from cloned cDNA and in HSV-infected cells. In addition, HSV-gE cycles between the TGN and the cell surface and requires a conserved tyrosine-containing motif within its cytoplasmic tail for proper trafficking. These results show that VZV-gE and HSV-gE have similar intracellular trafficking pathways, probably reflecting the presence of similar sorting signals in the cytoplasmic domains of both molecules, and suggest that the respective viruses, VZV and HSV, could use the same subcellular organelle, the TGN, for their envelopment. |
Databáze: | OpenAIRE |
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