ArticleJournal of virology2010
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.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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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
21 citing papers in PubMed, 30 citations in OpenAlex.
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
- Zyxin restricts viral fusion and entry across multiple virus families.Journal of virology · 2025Article
- A critical review on antiviral peptides derived from viral glycoproteins and host receptors to decoy herpes simplex virus.Microbial biotechnology · 2023Review
- Review
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Expression of the Pseudorabies Virus gB Glycoprotein Triggers NK Cell Cytotoxicity and Increases Binding of the Activating NK Cell Receptor PILRβ.Journal of virology · 2019Article
- Ephrin Receptor A4 is a New Kaposi's Sarcoma-Associated Herpesvirus Virus Entry Receptor.mBio · 2019Article
- Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Scientific reports · 2017Article
- Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry.Virology journal · 2015Article
- Cell entry mechanisms of HSV: what we have learned in recent years.Future virology · 2015Article
- Article
- Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- PILRα and PILRβ have a siglec fold and provide the basis of binding to sialic acid.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Drosophila Schneider 2 (S2) cells: a novel tool for studying HSV-induced membrane fusion.Virology · 2013Article
- A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Virology · 2013Article
- Neutrophil infiltration during inflammation is regulated by PILRα via modulation of integrin activation.Nature immunology · 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
- Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry.Journal of virology · 2012Article
- Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).Virology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Paired immunoglobulin (Ig)-like type 2 receptor alpha (PILRalpha) and PILRbeta are paired receptors that are highly homologous to each other. When engaged by ligand, PILRalpha is inhibitory whereas PILRbeta is activating. PILRalpha is a newly identified herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) receptor and is associated with membrane fusion and entry activity of HSV-1. PILRalpha is a 303-amino-acid protein with an Ig-like V (variable)-type domain from amino acid 31 to 150, whereas PILRbeta is a 217-amino-acid protein with an Ig-like V-type domain from amino acid 21 to 143. We report that PILRbeta is not a receptor for HSV-1 and HSV-2. Domain swaps between PILRalpha and PILRbeta reveal that the Ig-like V-type domain of PILRalpha, but not PILRbeta, plays a critical role in cell membrane fusion activity and the binding of PILRalpha to gB. Individual replacement of 13 amino acids in PILRalpha showed that most of these mutations had no effect on cell fusion activity. However, mutation of the tryptophan residue at amino acid 139 significantly impaired cell fusion activity for HSV-1 and eliminated binding to gB.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.