ArticleJournal of virology2009
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.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed.
- Article
- Zyxin restricts viral fusion and entry across multiple virus families.Journal of virology · 2025Article
- Article
- H84T BanLec has broad spectrum antiviral activity against human herpesviruses in cells, skin, and mice.Scientific reports · 2022Article
- Herpes Simplex Virus Glycoprotein B Mutations Define Structural Sites in Domain I, the Membrane Proximal Region, and the Cytodomain That Regulate Entry.Journal of virology · 2021Article
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Dual Ligand Insertion in gB and gD of Oncolytic Herpes Simplex Viruses for Retargeting to a Producer Vero Cell Line and to Cancer Cells.Journal of virology · 2018Article
- Article
- Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Scientific reports · 2017Article
- Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion.Journal of virology · 2014Article
- Cellular unfolded protein response against viruses used in gene therapy.Frontiers in microbiology · 2014Review
- Drosophila Schneider 2 (S2) cells: a novel tool for studying HSV-induced membrane fusion.Virology · 2013Article
- Amino acid differences in glycoproteins B (gB), C (gC), H (gH) and L (gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α.Virology journal · 2012Article
- Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands.The Journal of biological chemistry · 2012Article
- Review
- Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry.Journal of virology · 2012Article
- Bispecific adapter-mediated retargeting of a receptor-restricted HSV-1 vector to CEA-bearing tumor cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2011Article
- Article
- The Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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