ArticleProceedings of the National Academy of Sciences of the United States of America2005
The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
- The heterogeneous sensitivity of pediatric brain tumors to different oncolytic viruses is predicted by unique gene expression profiles.Molecular therapy. Oncology · 2024Article
- Pseudorabies gD protein protects mice and piglets against lethal doses of pseudorabies virus.Frontiers in microbiology · 2023Article
- Conformational Changes in Herpes Simplex Virus Glycoprotein C.Journal of virology · 2022Article
- Molecular determinants of the interaction between HSV-1 glycoprotein D and heparan sulfate.Frontiers in molecular biosciences · 2022Article
- Antibody Screening System Using a Herpes Simplex Virus (HSV)-Based Probe To Identify a Novel Target for Receptor-Retargeted Oncolytic HSVs.Journal of virology · 2021Article
- Crystal structure of bovine herpesvirus 1 glycoprotein D bound to nectin-1 reveals the basis for its low-affinity binding to the receptor.Science advances · 2020Article
- Article
- Oncolytic herpes simplex virus tumor targeting and neutralization escape by engineering viral envelope glycoproteins.Drug delivery · 2018Review
- Spotlight on… Gabriella Campadelli-Fiume.FEMS microbiology letters · 2018Article
- A novel glycoprotein D-specific monoclonal antibody neutralizes herpes simplex virus.Antiviral research · 2017Article
- Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.PLoS pathogens · 2017Article
- Syncytial Mutations Do Not Impair the Specificity of Entry and Spread of a Glycoprotein D Receptor-Retargeted Herpes Simplex Virus.Journal of virology · 2016Article
- Development of an oncolytic HSV vector fully retargeted specifically to cellular EpCAM for virus entry and cell-to-cell spread.Gene therapy · 2016Article
- Review
- Mutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Journal of virology · 2015Article
- The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its Receptors.PLoS pathogens · 2015Article
- Evasion of early antiviral responses by herpes simplex viruses.Mediators of inflammation · 2015Review
- Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Journal of virology · 2014Article
- Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1.Virology · 2014Article
5 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
Entry of herpes simplex virus into the cell requires the interaction of gD with one of its receptors, herpesvirus entry mediator or nectin 1, and the intervention of gB, gH, or gL, required to execute fusion of the virion envelope with cell membranes. The gD ectodomain is organized in two structurally and functionally differentiated regions. The N terminus (residues 1-260) carries the receptor binding sites, and the C terminus (residues 260-310) functions as the pro-fusion domain (PFD), which is required for viral infectivity and fusion but not for receptor binding. The objective of our studies is to elucidate how gD links receptor recognition to the triggering of fusion. Here, we show that PFD is made of subdomains 1 and 2 (amino acids 260-285 and 285-310). Each one partially contributed to herpes simplex virus infectivity. By means of glutathione S-transferase (GST) fusion proteins, we show that PFD bound soluble forms of gD, truncated at residue 260 (gD260t) or downstream. Both PFD subdomains bound gD260t, highlighting multiple contact sites between the N and C termini of gD. When gD260t was in complex with either receptor, it failed to bind GST-PFD. In turn, the receptors did not bind GST-PFD, irrespective of whether they were in complex with gD. Thus, gD260t interacted with the C terminus only if unbound to the receptor. We propose that (i) before receptor binding, gD adopts a "closed" conformation in which the N and C termini interact; and (ii) on encounter with a receptor, gD modifies its conformation and the N and C termini are released from reciprocal interactions ("opened" conformation) and enabled to trigger fusion.
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