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Journal of Virology, October 2009, p. 10752-10760, Vol. 83, No. 20
0022-538X/09/$08.00+0     doi:10.1128/JVI.01287-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Cross Talk among the Glycoproteins Involved in Herpes Simplex Virus Entry and Fusion: the Interaction between gB and gH/gL Does Not Necessarily Require gD{triangledown}

Elisa Avitabile, Cristina Forghieri,{dagger} and Gabriella Campadelli-Fiume*

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

Received 23 June 2009/ Accepted 23 July 2009

The gD, gB, and gH/gL glycoprotein quartet constitutes the basic apparatus for herpes simplex virus (HSV) entry into the cell and fusion. gD serves as a receptor binding glycoprotein and trigger of fusion. The conserved gB and gH/gL execute fusion. Central to understanding HSV entry/fusion has become the dissection of how the four glycoproteins engage in cross talk. While the independent interactions of gD with gB and gD with gH/gL have been documented, less is known of the interaction of gB with gH/gL. So far, this interaction has been detected only in the presence of gD by means of a split green fluorescent protein complementation assay. Here, we show that gB interacts with gH/gL in the absence of gD. The gB-gH/gL complex was best detected with a form of gB in which the endocytosis and phosphorylation motif have been deleted; this form of gB persists in the membranes of the exocytic pathway and is not endocytosed. The gB-gH/gL interaction was detected both in whole transfected cells by means of a split yellow fluorescent protein complementation assay and, biochemically, by a pull-down assay. Results with a panel of chimeric forms of gB, in which portions of the glycoprotein bracketed by consecutive cysteines were replaced with the corresponding portions from human herpesvirus 8 gB, favor the view that gB carries multiple sites for interaction with gH/gL, and one of these sites is located in the pleckstrin-like domain 1 carrying the bipartite fusion loop.

* Corresponding author. Mailing address: Department of Experimental Pathology, Section on Microbiology and Virology, Alma Mater Studiorum—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 5 August 2009.

{dagger} Present address: Department of Biomedical Sciences, Modena e Reggio Emilia University, Modena, Italy.

Journal of Virology, October 2009, p. 10752-10760, Vol. 83, No. 20
0022-538X/09/$08.00+0     doi:10.1128/JVI.01287-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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