PMID: 9658112Jul 11, 1998Paper

Steady-state plasma membrane expression of human cytomegalovirus gB is determined by the phosphorylation state of Ser900

Journal of Virology
K N FishJ A Nelson

Abstract

Human cytomegalovirus (HCMV) infection of an astrocytoma cell line (U373) or human fibroblast (HF) cells results in a differential cell distribution of the major envelope glycoprotein gB (UL55). This 906-amino-acid type I glycoprotein contains an extracellular domain with a signal sequence, a transmembrane domain, and a 135-amino-acid cytoplasmic tail with a consensus casein kinase II (CKII) site located at Ser900. Since phosphorylation of proteins in the secretory pathway is an important determinant of intracellular trafficking, the state of gB phosphorylation in U373 and HF cells was examined. Analysis of cells expressing wild-type gB and gB with site-specific mutations indicated that the glycoprotein was equally phosphorylated at a single site, Ser900, in both U373 and HF cells. To assess the effect of charge on gB surface expression in U373 cells, Ser900 was replaced with an aspartate (Asp) or alanine (Ala) residue to mimic the phosphorylated and nonphosphorylated states, respectively. Expression of the Asp but not the Ala gB mutation resulted in an increase in the steady-state expression of gB at the plasma membrane (PM) in U373 cells. In addition, treatment of U373 cells with the phosphatase inhibitor tautomycin resulted ...Continue Reading

Citations

Feb 11, 2004·The Journal of General Virology·Manohara S Mavinakere, Anamaris M Colberg-Poley
Aug 6, 2005·Cytometry. Part a : the Journal of the International Society for Analytical Cytology·Robert F Murphy
Sep 23, 1998·The Journal of Cell Biology·S S MolloyG Thomas
Nov 3, 2006·Journal of Virology·Emmanuel J WiertzMaaike E Ressing

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