ArticleProceedings of the National Academy of Sciences of the United States of America2004
Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 96 citations in OpenAlex.
- Complete disruption of gD binding to HVEM alters virus replication and host receptor homeostasis.PLoS pathogens · 2026Article
- HSV-1 strain H129 co-opts neuronal synaptic transmission machinery for its transsynaptic spread.Nature neuroscience · 2026Article
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
- Glycocalyx at the host-virus interface: a double-edged sword in virus infection and tissue damage.Frontiers in molecular biosciences · 2026Review
- Cell Intrinsic Determinants of Alpha Herpesvirus Latency and Pathogenesis in the Nervous System.Viruses · 2023Review
- Novel mutations in UMolecular therapy. Methods & clinical development · 2023Article
- Harnessing the Potential of Biosurfactants for Biomedical and Pharmaceutical Applications.Pharmaceutics · 2023Review
- Crystal structures of glycoprotein D of equine alphaherpesviruses reveal potential binding sites to the entry receptor MHC-I.Frontiers in microbiology · 2023Article
- Bioprocess development for biosurfactant production by Natrialba sp. M6 with effective direct virucidal and anti-replicative potential against HCV and HSV.Scientific reports · 2022Article
- Advancing Our Understanding of Corneal Herpes Simplex Virus-1 Immune Evasion Mechanisms and Future Therapeutics.Viruses · 2021Review
- Review
- Restoring Herpesvirus Entry Mediator (HVEM) Immune Function in HVEMJournal of virology · 2020Article
- 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
- TRPC1 participates in the HSV-1 infection process by facilitating viral entry.Science advances · 2020Article
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Mapping a highly conserved linear neutralizing epitope on gD glycoprotein of bovine herpesvirus type I using a monoclonal antibody.The Journal of veterinary medical science · 2019Article
- Herpesvirus Entry Mediator and Ocular Herpesvirus Infection: More than Meets the Eye.Journal of virology · 2017Review
- Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Scientific reports · 2017Article
- Herpes simplex virus Membrane Fusion.Advances in anatomy, embryology, and cell biology · 2017Review
- A Herpes Simplex Virus 2 (HSV-2) gD Mutant Impaired for Neural Tropism Is Superior to an HSV-2 gD Subunit Vaccine To Protect Animals from Challenge with HSV-2.Journal of virology · 2016Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Glycoprotein D (gD) determines which cells can be infected by herpes simplex virus (HSV) by binding to one of the several cell surface receptors that can mediate HSV entry or cell fusion. These receptors include the herpesvirus entry mediator (HVEM), nectin-1, nectin-2, and sites in heparan sulfate generated by specific 3-O-sulfotransferases. The objective of the present study was to identify residues in gD that are critical for physical and functional interactions with nectin-1 and nectin-2. We found that double or triple amino acid substitutions at positions 215, 222, and 223 in gD caused marked reduction in gD binding to nectin-1 and a corresponding inability to function in cell fusion or entry of HSV via nectin-1 or nectin-2. These substitutions either enhanced or did not significantly inhibit functional interactions with HVEM and modified heparan sulfate. These and other results demonstrate that different domains of gD, with some overlap, are critical for functional interactions with each class of entry receptor. Viral entry assays, using gD mutants described here and previously, revealed that nectins are the principal entry receptors for selected human cell lines of neuronal and epithelial origin, whereas HVEM or nectins could be used to mediate entry into a T lymphocyte line. Because T cells and fibroblasts can be infected via HVEM, HSV strains carrying gD mutations that prevent entry via nectins may establish transient infections in humans, but perhaps not latent infections of neurons, and are therefore candidates for development of safe live virus vaccines and vaccine vectors.
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