ArticleProceedings of the National Academy of Sciences of the United States of America2007
Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Signal peptide cleavage and ectodomain regions of GP2 are required for PRRSV infection.The Journal of general virology · 2026Article
- Oncolytic herpes simplex viruses designed for targeted treatment of EGFR-bearing tumors.Molecular therapy. Oncology · 2024Article
- Targeted Delivery of IL-12 Adjuvants Immunotherapy by Oncolytic Viruses.Advances in experimental medicine and biology · 2021Article
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- Oncolytic herpes simplex virus tumor targeting and neutralization escape by engineering viral envelope glycoproteins.Drug delivery · 2018Review
- 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
- Simultaneous Insertion of Two Ligands in gD for Cultivation of Oncolytic Herpes Simplex Viruses in Noncancer Cells and Retargeting to Cancer Receptors.Journal of virology · 2018Article
- A Strategy for Cultivation of Retargeted Oncolytic Herpes Simplex Viruses in Non-cancer Cells.Journal of virology · 2017Article
- Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Scientific reports · 2017Article
- Retargeting of herpes simplex virus (HSV) vectors.Current opinion in virology · 2016Review
- Review
- The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its Receptors.PLoS pathogens · 2015Article
- Oncolytic virotherapy using herpes simplex virus: how far have we come?Oncolytic virotherapy · 2015Review
- Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Journal of virology · 2014Article
- New viruses for cancer therapy: meeting clinical needs.Nature reviews. Microbiology · 2014Review
- Effective treatment of an orthotopic xenograft model of human glioblastoma using an EGFR-retargeted oncolytic herpes simplex virus.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- Targeted entry of enveloped viruses: measles and herpes simplex virus I.Current opinion in virology · 2012Review
- Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion.Nature communications · 2011Article
- Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.PLoS pathogens · 2011Article
- Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain.The Journal of biological chemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The 369-residue glycoprotein D (gD) is the entry, receptor-binding protein of herpes simplex virus 1. The common receptors for viral entry are nectin-1, HveA, and a specific O-linked sulfated proteoglycan. The major receptor-binding sites of gD are at the N terminus, whereas the domain required for fusion of viral envelope with the plasma membrane is at the C terminus of the ectodomain (residues 260-310). In the course of retargeting gD to the urokinase plasminogen activator (uPA) receptor for potential therapeutic applications, we obtained a genetically engineered infectious virus in which the receptor-binding domain consisting of the N-terminal domain of uPA fused to residues 33-60 of gD was separated from an independently expressed C-terminal domain of gD containing residues 219-369. The intervening sequences (residues 62-218) were replaced by a stop codon and a promoter for the C-terminal domain of gD. The physical interaction of the two components was reconstructed by coimmunoprecipitation of the N-terminal domain of uPA with the C-terminal domain of gD. These results indicate that codons 61-218 of gD do not encode executable functions required for viral entry into cells and suggest that the receptor-binding ligand must interact with but need not alter the structure of the residual portion of gD to effect virus entry. This finding opens the way for the development of a family of recombinant viruses in which the profusion domain of gD and independently furnished, interacting receptor-binding domains effect entry of the virus via a range of receptors.
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