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Journal of Virology, January 2006, p. 138-148, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.138-148.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Soluble V Domain of Nectin-1/HveC Enables Entry of Herpes Simplex Virus Type 1 (HSV-1) into HSV-Resistant Cells by Binding to Viral Glycoprotein D

Heechung Kwon,1,2,{dagger} Qing Bai,1,{dagger} Hyun-Jung Baek,2 Kelly Felmet,1 Edward A. Burton,1 William F. Goins,1 Justus B. Cohen,1 and Joseph C. Glorioso1*

Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261,1 Laboratory of Molecular Oncology, Korea Institute of Radiological and Medical Sciences, Seoul, South Korea2

Received 26 June 2005/ Accepted 21 September 2005

Interaction of herpes simplex virus (HSV) glycoprotein D (gD) with specific cellular receptors is essential for HSV infection of susceptible cells. Virus mutants that lack gD can bind to the cell surface (attachment) but do not enter, implying that interaction of gD with its receptor(s) initiates the postattachment (entry) phase of HSV infection. In this report, we have studied HSV entry in the presence of the gD-binding variable (V) domain of the common gD receptor nectin-1/HveC to determine whether cell association of the gD receptor is required for HSV infection. In the presence of increasing amounts of the soluble nectin-1 V domain (sNec1123), increasing viral entry into HSV-resistant CHO-K1 cells was observed. At a multiplicity of 3 in the presence of optimal amounts of sNec1123, approximately 90% of the cells were infected. The soluble V domain of nectin-2, a strain-specific HSV entry receptor, promoted entry of the HSV type 1 (HSV-1) Rid-1 mutant strain, but not of wild-type HSV-1. Preincubation and immunofluorescence studies indicated that free or gD-bound sNec1123 did not associate with the cell surface. sNec1123-mediated entry was highly impaired by interference with the cell-binding activities of viral glycoproteins B and C. While gD has at least two functions, virus attachment to the cell and initiation of the virus entry process, our results demonstrate that the attachment function of gD is dispensable for entry provided that other means of attachment are available, such as gB and gC binding to cell surface glycosaminoglycans.

* Corresponding author. Mailing address: University of Pittsburgh, School of Medicine, Department of Molecular Genetics and Biochemistry, E1246 Biomedical Science Tower, Pittsburgh, PA 15261. Phone: (412) 648-8105. Fax: (412) 624-8997. E-mail: glorioso{at}pitt.edu.

{dagger} H.K. and Q.B. contributed equally to this work.

Journal of Virology, January 2006, p. 138-148, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.138-148.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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