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Title: Intracellular transport and stability of varicella-zoster virus glycoprotein K

Abstract

VZV gK, an essential glycoprotein that is conserved among the alphaherpesviruses, is believed to participate in membrane fusion and cytoplasmic virion morphogenesis based on analogy to its HSV-1 homolog. However, the production of VZV gK-specific antibodies has proven difficult presumably due to its highly hydrophobic nature and, therefore, VZV gK has received limited study. To overcome this obstacle, we inserted a FLAG epitope into gK near its amino terminus and produced VZV recombinants expressing epitope-tagged gK (VZV gK-F). These recombinants grew indistinguishably from native VZV, and FLAG-tagged gK could be readily detected in VZV gK-F-infected cells. FACS analysis established that gK is transported to the plasma membrane of infected cells, while indirect immunofluorescence demonstrated that gK accumulates predominately in the Golgi. Using VZV gK-F-infected cells we demonstrated that VZV gK, like several other herpesvirus glycoproteins, is efficiently endocytosed from the plasma membrane. However, pulse-labeling experiments revealed that the half-life of gK is considerably shorter than that of other VZV glycoproteins including gB, gE and gH. This finding suggests that gK may be required in lower abundance than other viral glycoproteins during virion morphogenesis or viral entry.

Authors:
 [1];  [1];  [2]
  1. Division of Infectious Diseases and Immunology, Saint Louis University School of Medicine, Saint Louis, Missouri 63110-0250 (United States)
  2. Division of Infectious Diseases and Immunology, Saint Louis University School of Medicine, Saint Louis, Missouri 63110-0250 (United States). E-mail: heinemtc@slu.edu
Publication Date:
OSTI Identifier:
20975213
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 358; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2006.08.021; PII: S0042-6822(06)00579-4; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANTIBODIES; CELL MEMBRANES; GLYCOPROTEINS; HALF-LIFE; LABELLING; MORPHOGENESIS; VIRUSES

Citation Formats

Hall, Susan L., Govero, Jennifer L., and Heineman, Thomas C. Intracellular transport and stability of varicella-zoster virus glycoprotein K. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.08.021.
Hall, Susan L., Govero, Jennifer L., & Heineman, Thomas C. Intracellular transport and stability of varicella-zoster virus glycoprotein K. United States. doi:10.1016/j.virol.2006.08.021.
Hall, Susan L., Govero, Jennifer L., and Heineman, Thomas C. Tue . "Intracellular transport and stability of varicella-zoster virus glycoprotein K". United States. doi:10.1016/j.virol.2006.08.021.
@article{osti_20975213,
title = {Intracellular transport and stability of varicella-zoster virus glycoprotein K},
author = {Hall, Susan L. and Govero, Jennifer L. and Heineman, Thomas C.},
abstractNote = {VZV gK, an essential glycoprotein that is conserved among the alphaherpesviruses, is believed to participate in membrane fusion and cytoplasmic virion morphogenesis based on analogy to its HSV-1 homolog. However, the production of VZV gK-specific antibodies has proven difficult presumably due to its highly hydrophobic nature and, therefore, VZV gK has received limited study. To overcome this obstacle, we inserted a FLAG epitope into gK near its amino terminus and produced VZV recombinants expressing epitope-tagged gK (VZV gK-F). These recombinants grew indistinguishably from native VZV, and FLAG-tagged gK could be readily detected in VZV gK-F-infected cells. FACS analysis established that gK is transported to the plasma membrane of infected cells, while indirect immunofluorescence demonstrated that gK accumulates predominately in the Golgi. Using VZV gK-F-infected cells we demonstrated that VZV gK, like several other herpesvirus glycoproteins, is efficiently endocytosed from the plasma membrane. However, pulse-labeling experiments revealed that the half-life of gK is considerably shorter than that of other VZV glycoproteins including gB, gE and gH. This finding suggests that gK may be required in lower abundance than other viral glycoproteins during virion morphogenesis or viral entry.},
doi = {10.1016/j.virol.2006.08.021},
journal = {Virology},
number = 2,
volume = 358,
place = {United States},
year = {Tue Feb 20 00:00:00 EST 2007},
month = {Tue Feb 20 00:00:00 EST 2007}
}