Membrane fusion mediated by herpesvirus glycoproteins: the paradigm of varicella-zoster virus
Abstract
Varicella‐zoster virus (VZV) is well known for its propensity to cause polykaryons (syncytia) in the vesicles within infected skin. Similarly in cultured cells, VZV induces extensive syncytial formation by virus‐mediated cell‐to‐cell fusion. Statistical analyses of fusion parameters demonstrated three‐way interactive effects among all three tested variables (incubation temperature, cell type and virus strain). For example, fusion was greatly enhanced at 33°C vs 37°C; also fusion was pronounced in epidermal cells but negligible in fibroblast cells. As with all herpesviruses, VZV gH was a major fusogen. VZV cell fusion was inhibited by antibody to gH, but surprisingly was enhanced by antibody to gE. Other evidence implicating a role for VZV gE in the fusion process was provided by two mutant viruses, in which gE cell surface expression was enhanced. Under transfection conditions, VZV fusion formation occurred after expression of the gH/gL complex; in contrast, pseudorabies virus requires expression of gH, gL and gB, while the herpes simplex virus (HSV) types 1 and 2 require the quartet of gH, gL, gB and gD. VZV has no gD gene and no apparent gD functional homologue. On the other hand, VZV gE exerts a greater effect than HSV gE on membrane fusion. Taken together, the data in this review suggest that VZV has evolved viral glycoprotein machinery more geared toward cell‐to‐cell fusion (fusion‐from‐within) than toward virus‐to‐cell fusion (entry/fusion‐from‐without), as a means for syncytium formation within the human epidermis. Copyright © 2003 John Wiley & Sons, Ltd.
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Cell-cell fusion, synapse formation, filopodial bridges, and nanotubes have been documented for cytomegaloviruses, varicella zoster virus, pseudorabies virus, and herpes simplex virus.
“Cell-cell fusion, synapse formation, filopodial bridges, and nanotubes were documented for cytomegaloviruses (CMV), varicella zoster virus (VZV), pseudorabies virus (PRV), and herpes simplex virus (HSV-1) (Cole and Grose, 2003; Dingwell et al., 1994; Favoreel et al., 2005; Gerna et al., 2000; Sweet, 1999; van Leeuwen et al., 2002).”
From Equid Herpesvirus-1 Exploits the Extracellular Matrix of Mononuclear Cells to Ensure Transport to Target Cells (2020) · cites this paper as Cole and Grose, 2003
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- Authors
- Cole, N. L., & Grose, C.
- Affiliations
- University of Iowa (US)
- Corresponding author
- Grose, Charles
- ORCID
- Grose, Charles
- Venue
- Reviews in Medical Virology
- Publisher
- Wiley
- Published
- 2003-06-17
- Volume
- 13
- Issue
- 4
- Pages
- 207-222
- ISSN
- 1052-9276 (ISSN-L)
- 1099-1654
- OpenAlex
- W2060968666
- Cited by
- 112
- References
- 76
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 7 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 4 · 2014: 6 · 2013: 3 · 2012: 3
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Reviews in Medical Virology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI 22795, AI 36884, R01AI022795)
- Topics
- Health Sciences › Medicine › Epidemiology › Herpesvirus Infections and Treatments
- Health Sciences › Medicine › Epidemiology › Cytomegalovirus and herpesvirus research
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- varicella-zoster virus, herpesvirus glycoproteins, membrane fusion, syncytium formation, gH/gL complex, Ge, glycoprotein B, gadolinium, cell-to-cell fusion, viral entry, epidermal cells, herpesvirus evolution
- MeSH terms
- Cells, Cultured, Biological Evolution, Herpesviridae, Humans, Membrane Fusion, Membrane Glycoproteins, Microscopy, Electron, Temperature, Transfection, Herpesvirus 3, Human, Viral Envelope Proteins, Viral Matrix Proteins, Viral Proteins, Giant Cells
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