ArticlePLoS pathogens2011
Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.
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Who cites it
129 citing papers in PubMed, 185 citations in OpenAlex.
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- Pre-assembled complexes and allosteric effects: parallels between eukaryotic phosphorylation cascades and membrane fusion during herpesviral entry.Journal of virology · 2026Review
- Rare missense variants inFrontiers in genetics · 2026Article
- Molecular characterization of infectious laryngotracheitis virus in China and host transcriptomic responses to immunization with a live attenuated vaccine.Archives of virology · 2025Article
- Small molecule UCM05 inhibits HSV-2 infection via targeting viral glycoproteins and fatty acid synthase with potentiating antiviral immunity.Virology journal · 2025Article
- A potent protective bispecific nanobody targeting Herpes simplex virus gD reveals vulnerable epitope for neutralizing.Nature communications · 2025Article
- Herpes simplex virus 1 envelope glycoprotein C shields glycoprotein D to protect virions from entry-blocking antibodies.Journal of virology · 2025Article
- Article
- Infectious Laryngotracheitis Virus and Avian Metapneumovirus: A Comprehensive Review.Pathogens (Basel, Switzerland) · 2025Review
- Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024Article
- Nectin1 is a pivotal host factor involved in attachment and entry of red-spotted grouper nervous necrosis virus in the early stages of the viral life cycle.Journal of virology · 2024Article
- Herpes Simplex Virus 1 Envelope Glycoprotein C Shields Glycoprotein D to Protect Virions from Entry-Blocking Antibodies.bioRxiv : the preprint server for biology · 2024Article
- Oncolytic herpes simplex viruses designed for targeted treatment of EGFR-bearing tumors.Molecular therapy. Oncology · 2024Article
- Single amino acid mutation of nectin-1 provides remarkable resistance against lethal pseudorabies virus infection in mice.The Journal of veterinary medical science · 2024Article
- Virus-Induced Cell Fusion and Syncytia Formation.Results and problems in cell differentiation · 2024Article
- Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.Nature communications · 2023Article
- Rapid and accurate detection of herpes simplex virus type 2 using a low-cost electrochemical biosensor.Cell reports. Physical science · 2023Article
- NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Towards a comprehensive view of the herpes B virus.Frontiers in immunology · 2023Review
69 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells. Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells. We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution. The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor. A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions. Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex. Notably, mutation of Phe129 to alanine prevents nectin-1 binding to gD and HSV entry. Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions. Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
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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.