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Journal of Virology, October 2001, p. 9483-9492, Vol. 75, No. 19
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.19.9483-9492.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Varicella-Zoster Virus gB and gE Coexpression, but Not gB or gE Alone, Leads to Abundant Fusion and Syncytium Formation Equivalent to Those from gH and gL Coexpression

Lucie Maresova, Tracy Jo Pasieka, and Charles Grose*

Departments of Microbiology and Pediatrics, University of Iowa, Iowa City, Iowa

Received 10 April 2001/Accepted 3 July 2001

Varicella-zoster virus (VZV) is distinguished from herpes simplex virus type 1 (HSV-1) by the fact that cell-to-cell fusion and syncytium formation require only gH and gL within a transient-expression system. In the HSV system, four glycoproteins, namely, gH, gL, gB, and gD, are required to induce a similar fusogenic event. VZV lacks a gD homologous protein. In this report, the role of VZV gB as a fusogen was investigated and compared to the gH-gL complex. First of all, the VZV gH-gL experiment was repeated under a different set of conditions; namely, gH and gL were cloned into the same vaccinia virus (VV) genome. Surprisingly, the new expression system demonstrated that a recombinant VV-gH+gL construct was even more fusogenic than seen in the prior experiment with two individual expression plasmids containing gH and gL (K. M. Duus and C. Grose, J. Virol. 70:8961-8971, 1996). Recombinant VV expressing VZV gB by itself, however, effected the formation of only small syncytia. When VZV gE and gB genes were cloned into one recombinant VV genome and another fusion assay was performed, extensive syncytium formation was observed. The degree of fusion with VZV gE-gB coexpression was comparable to that observed with VZV gH-gL: in both cases, >80% of the cells in a monolayer were fused. Thus, these studies established that VZV gE-gB coexpression greatly enhanced the fusogenic properties of gB. Control experiments documented that the fusion assay required a balance between the fusogenic potential of the VZV glycoproteins and the fusion-inhibitory effect of the VV infection itself.

* Corresponding author. Mailing address: University of Iowa Hospital/2501 JCP, 200 Hawkins Dr., Iowa City, IA 52242. Phone: (319) 356-2288. Fax: (319) 356-4855. E-mail: charles-grose{at}uiowa.edu.

Journal of Virology, October 2001, p. 9483-9492, Vol. 75, No. 19
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.19.9483-9492.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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