ArticlePLoS pathogens2019
Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells.Nature microbiology · 2025Article
- Single-molecule localisation microscopy approaches reveal envelope glycoprotein clusters in single-enveloped viruses: a potential functional role?Biochemical Society transactions · 2025Review
- Resolving viral structural complexity by super-resolution microscopy.Archives of virology · 2024Review
- Resolving the differential distribution of structural proteins in baculovirus using single-molecule localization microscopy.The Journal of general virology · 2024Article
- An updated review of HSV-1 infection-associated diseases and treatment, vaccine development, and vector therapy application.Virulence · 2024Review
- Viral Attachment Blocking Chimera Composed of DNA Origami and Nanobody Inhibits Pseudorabies Virus Infection In Vitro.ACS nano · 2023Article
- Mechanistic Understanding of the Antiviral Properties of Pistachios and Zeaxanthin against HSV-1.Viruses · 2023Article
- Article
- Virus morphology: Insights from super-resolution fluorescence microscopy.Biochimica et biophysica acta. Molecular basis of disease · 2022Review
- Interaction Mechanism Between the HSV-1 Glycoprotein B and the Antimicrobial Peptide Amyloid-β.Journal of Alzheimer's disease reports · 2022Article
- Release of HSV-1 Cell-Free Virions: Mechanisms, Regulation, and Likely Role in Human-Human Transmission.Viruses · 2021Review
- Studying SARS-CoV-2 with Fluorescence Microscopy.International journal of molecular sciences · 2021Review
- Towards a Quantitative Single Particle Characterization by Super Resolution Microscopy: From Virus Structures to Antivirals Design.Frontiers in bioengineering and biotechnology · 2021Review
- Elucidating the microscopic and computational techniques to study the structure and pathology of SARS-CoVs.Microscopy research and technique · 2020Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins must be located at the point of contact between cellular and viral envelopes to interact and allow fusion. Using super-resolution microscopy, we show that gB, gH/gL and most of gC are distributed evenly round purified virions. In contrast, gD localizes essentially as clusters which are distinct from gB and gH/gL. Upon cell binding, we observe that all glycoproteins, including gD, have a similar ring-like pattern, but the diameter of these rings was significantly smaller than those observed on cell-free viruses. We also observe that contrary to cell-free particles, gD mostly colocalizes with other glycoproteins on cell-bound particles. The differing patterns of localization of gD between cell-free and cell-bound viruses indicates that gD can be reorganized on the viral envelope following either a possible maturation of the viral particle or its adsorption to the cell. This redistribution of glycoproteins upon cell attachment could contribute to initiate the cascade of activations leading to membrane fusion.
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Registered trials
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