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Journal of Virology, March 2004, p. 2884-2896, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.2884-2896.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Regulation of Varicella-Zoster Virus-Induced Cell-to-Cell Fusion by the Endocytosis-Competent Glycoproteins gH and gE

Tracy Jo Pasieka,1 Lucie Maresova,1 Kimiyasu Shiraki,2 and Charles Grose1*

Department of Pediatrics, University of Iowa College of Medicine, Iowa City, Iowa,1 Department of Virology, Toyama Medical and Pharmaceutical University, Toyama, Japan2

Received 25 August 2003/ Accepted 20 November 2003

The gH glycoprotein of varicella-zoster virus (VZV) is a major fusogen. The realigned short cytoplasmic tail of gH (18 amino acids) harbors a functional endocytosis motif (YNKI) that mediates internalization in both VZV-infected and transfected cells (T. J. Pasieka, L. Maresova, and C. Grose, J. Virol. 77: 4194-4202, 2003). During subsequent confocal microscopy studies of endocytosis-deficient gH mutants, we observed that cells transfected with the gH tail mutants exhibited marked fusion. Therefore, we postulated that VZV gH endocytosis served to regulate cell-to-cell fusion. Subsequent analyses of gH+gL transfection fusion assays by the Kolmogorov-Smirnov statistical test demonstrated that expression of the endocytosis-deficient gH mutants resulted in a statistically significant enhancement of cell-to-cell fusion (P < 0.0001) compared to wild-type gH. On the other hand, coexpression of VZV gE, another endocytosis-competent VZV glycoprotein, was able to temper the fusogenicity of the gH endocytosis mutants by facilitating internalization of the mutant gH protein from the cell surface. When the latter results were similarly analyzed, there was no longer any enhanced fusion by the endocytosis-deficient gH mutant protein. In summary, these studies support a role for gH endocytosis in regulating the cell surface expression of gH and thereby regulating gH-mediated fusion. The data also confirm and extend prior observations of a gE-gH interaction during viral glycoprotein trafficking in a VZV transfection system.

* Corresponding author. Mailing address: University of Iowa Hospital/2501 JCP, 200 Hawkins Dr., Iowa City, IA 52242. Phone: (319) 356-2270. Fax: (319) 356-4855. E-mail: charles-grose{at}uiowa.edu.

Journal of Virology, March 2004, p. 2884-2896, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.2884-2896.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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