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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.

Abstract：

: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 (PILRalpha) was identified as a receptor for HSV type 1 (HSV-1) gB. Both PILRalpha 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 PILRalpha 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 PILRalpha was overexpressed much more than when nectin-1 was overexpressed. Most of the insertions reduced the binding of gB to PILRalpha, for at least some forms of gB, but this reduction did not necessarily correlate with the selective reduction in cell fusion activity with PILRalpha. These results suggest that the regions targeted by the relevant mutations are critical for functional activity with PILRalpha. 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.

journal_name

J Virol

journal_title

Journal of virology

authors

Fan Q,Lin E,Satoh T,Arase H,Spear PG

doi

10.1128/JVI.00087-09

subject

Has Abstract

pub_date

2009-08-01 00:00:00

pages

7384-90

issue

15

eissn

0022-538X

issn

1098-5514

pii

JVI.00087-09

journal_volume

83

pub_type

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