This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Google Scholar Articles by Fan, Q. Articles by Spear, P. G. PubMed PubMed Citation Articles by Fan, Q. Articles by Spear, P. G.

 Previous Article  |  Next Article 

Journal of Virology, August 2009, p. 7384-7390, Vol. 83, No. 15
0022-538X/09/$08.00+0     doi:10.1128/JVI.00087-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Differential Effects on Cell Fusion Activity of Mutations in Herpes Simplex Virus 1 Glycoprotein B (gB) Dependent on Whether a gD Receptor or a gB Receptor Is Overexpressed

Qing Fan,¹ Erick Lin,¹ Takeshi Satoh,² Hisashi Arase,² and Patricia G. Spear^1*

Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611,¹ Department of Immunochemistry, Research Institute for Microbial Diseases, and Laboratory of Immunochemistry, WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan²

Received 14 January 2009/ Accepted 16 May 2009

Glycoprotein B (gB) of herpes simplex virus (HSV) is one of four glycoproteins essential for viral entry and cell fusion. Recently, paired immunoglobulin-like type 2 receptor (PILR) was identified as a receptor for HSV type 1 (HSV-1) gB. Both PILR and a gD receptor were shown to participate in HSV-1 entry into certain cell types. The purpose of this study was to determine whether insertional mutations in gB had differential effects on its function with PILR and the gD receptor, nectin-1. Previously described gB mutants and additional newly characterized mutants were used in this study. We found that insertional mutations near the N terminus and C terminus of gB and especially in the central region of the ectodomain reduced cell fusion activity when PILR was overexpressed much more than when nectin-1 was overexpressed. Most of the insertions reduced the binding of gB to PILR, for at least some forms of gB, but this reduction did not necessarily correlate with the selective reduction in cell fusion activity with PILR. These results suggest that the regions targeted by the relevant mutations are critical for functional activity with PILR. They also suggest that, although both the binding of gB to a gB receptor and the binding of gD to a gD receptor may be required for HSV-induced cell fusion, the two receptor-binding activities may have unequal weights in triggering fusogenic activity, depending on the ratios of gB and gD receptors or other factors.

---

* Corresponding author. Mailing address: Department of Microbiology-Immunology, Northwestern University, MC S213, 320 East Superior Street, Chicago, IL 60611. Phone: (312) 503-8230. Fax: (312) 503-1339. E-mail: p-spear{at}northwestern.edu

Published ahead of print on 20 May 2009.

---

Journal of Virology, August 2009, p. 7384-7390, Vol. 83, No. 15
0022-538X/09/$08.00+0     doi:10.1128/JVI.00087-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Wang, J., Fan, Q., Satoh, T., Arii, J., Lanier, L. L., Spear, P. G., Kawaguchi, Y., Arase, H. (2009). Binding of Herpes Simplex Virus Glycoprotein B (gB) to Paired Immunoglobulin-Like Type 2 Receptor {alpha} Depends on Specific Sialylated O-Linked Glycans on gB. J. Virol. 83: 13042-13045 [Abstract] [Full Text]