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Journal of Virology, October 2007, p. 11532-11537, Vol. 81, No. 20
0022-538X/07/$08.00+0     doi:10.1128/JVI.01343-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Complexes between Herpes Simplex Virus Glycoproteins gD, gB, and gH Detected in Cells by Complementation of Split Enhanced Green Fluorescent Protein{triangledown}

Elisa Avitabile, Cristina Forghieri, and Gabriella Campadelli-Fiume*

Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy

Received 20 June 2007/ Accepted 25 July 2007

The interactions between herpes simplex virus gD and its nectin1 receptor or between gD, gB, and gH were analyzed by complementation of the N and C portions of split enhanced green fluorescent protein (EGFP) fused to the glycoproteins. The gDN-NectC complex was readily detected; the gDN-gCC complex was undetectable, highlighting the specificity of the assay. Split EGFP complementation was detected between proteins designated gDN+gHC, gDN+gBC, and gHN+gBC+wtgD (gB was deleted of endocytosis motifs), both in cells transfected with two-tree glycoproteins and in syncytia. The in situ assay provides evidence that gD interacts with gH and gB independently of each other and supports a model whereby gH and gB in complex exert their activities to gD.

* Corresponding author. Mailing address: Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy. Phone: 39 051 2094733. Fax: 39 051 2094735. E-mail: gabriella.campadelli{at}unibo.it

{triangledown} Published ahead of print on 1 August 2007.

Journal of Virology, October 2007, p. 11532-11537, Vol. 81, No. 20
0022-538X/07/$08.00+0     doi:10.1128/JVI.01343-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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