ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 86 citations in OpenAlex.
- Aminoquinoline surfen inhibits pseudorabies virus attachment by preventing the binding of glycoprotein C to heparan sulfate.Microbiology spectrum · 2026Article
- Bovine Lactoferrin Inhibits Pseudorabies Virus Attachment Through Blockade of Glycoprotein C-Heparan Sulfate Interaction.Transboundary and emerging diseases · 2026Article
- Eph receptor tyrosine kinases are functional entry receptors for murine gammaherpesvirus 68.PLoS pathogens · 2025Article
- Article
- Pseudorabies Virus Glycoproteins E and B Application in Vaccine and Diagnosis Kit Development.Vaccines · 2024Review
- Article
- Tumor Tropism of DNA Viruses for Oncolytic Virotherapy.Viruses · 2023Review
- Membrane fusion, potential threats, and natural antiviral drugs of pseudorabies virus.Veterinary research · 2023Review
- Article
- The Structures and Functions of VZV Glycoproteins.Current topics in microbiology and immunology · 2023Article
- Human herpesvirus 8 molecular mimicry of ephrin ligands facilitates cell entry and triggers EphA2 signaling.PLoS biology · 2021Article
- Potential neutralizing antibodies discovered for novel corona virus using machine learning.Scientific reports · 2021Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- Varicella-zoster virus: molecular controls of cell fusion-dependent pathogenesis.Biochemical Society transactions · 2020Review
- The Attenuated Pseudorabies Virus Vaccine Strain Bartha K61: A Brief Review on the Knowledge Gathered During 60 Years of Research.Pathogens (Basel, Switzerland) · 2020Review
- Functional Relevance of the Transmembrane Domain and Cytoplasmic Tail of the Pseudorabies Virus Glycoprotein H for Membrane Fusion.Journal of virology · 2018Article
- Functional Role of N-Linked Glycosylation in Pseudorabies Virus Glycoprotein gH.Journal of virology · 2018Article
- Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops.Journal of virology · 2018Article
- Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
3 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
10 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Compared with many well-studied enveloped viruses, herpesviruses use a more sophisticated molecular machinery to induce fusion of viral and cellular membranes during cell invasion. This essential function is carried out by glycoprotein B (gB), a class III viral fusion protein, together with the heterodimer of glycoproteins H and L (gH/gL). In pseudorabies virus (PrV), a porcine herpesvirus, it was shown that gH/gL can be substituted by a chimeric fusion protein gDgH, containing the receptor binding domain (RBD) of glycoprotein D fused to a truncated version of gH lacking its N-terminal domain. We report here the 2.1-Å resolution structure of the core fragment of gH present in this chimera, bound to the Fab fragment of a PrV gH-specific monoclonal antibody. The structure strongly complements the information derived from the recently reported structure of gH/gL from herpes simplex virus type 2 (HSV-2). Together with the structure of Epstein-Barr virus (EBV) gH/gL reported in parallel, it provides insight into potentially functional conserved structural features. One feature is the presence of a syntaxin motif, and the other is an extended "flap" masking a conserved hydrophobic patch in the C-terminal domain, which is closest to the viral membrane. The negative electrostatic surface potential of this domain suggests repulsive interactions with the lipid heads. The structure indicates the possible unmasking of an extended hydrophobic patch by movement of the flap during a receptor-triggered conformational change of gH, exposing a hydrophobic surface to interact with the viral membrane during the fusion process.
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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.