αVβ3-Integrin Relocalizes nectin1 and Routes Herpes Simplex Virus to Lipid Rafts
Open accessAbstract
Herpes simplex virus (HSV) enters cells by fusion at plasma membranes or endosomes. Cellular factors route the virus to different pathways. αVβ3-integrin directs HSV to a lipid raft and acidic endosome pathway. We report that infection mediated by nectin1 plus αVβ3-integrin exhibits the same characteristics as entry mediated by raft-located forms of nectin. αVβ3-integrin relocalizes nectin1 to lipid rafts, independently of virus. Thus, HSV routing to the lipid raft-dependent pathway is consequent to the integrin-induced relocalization of nectin1. Inhibition by the Na+/H+ exchanger 5-(N-ethyl-N-isopropyl)amirolide suggests that αVβ3-integrin overexpression favors HSV macropinocytic uptake in some cells but not in others.
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αvβ3 integrin acts as a co-receptor for HSV1 and HCMV.
“αvβ3 integrin acts as a co-receptor for HSV1 and HCMV (Wang et al., 2005; Gianni and Campadelli-Fiume, 2012).”
From The Pathogenesis and Immune Evasive Mechanisms of Equine Herpesvirus Type 1 (2021) · cites this paper as Gianni and Campadelli-Fiume, 2012
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Mercer, J., Schelhaas, M., & Helenius, A. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-104626 · Cited by 1,057 · see citing works
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The Pathogenesis and Immune Evasive Mechanisms of Equine Herpesvirus Type 1
Laval, K., Poelaert, K. C. K., Van Cleemput, J., Zhao, J., Vandekerckhove, A. P., Gryspeerdt, A. C., Garré, B., van der Meulen, K., Baghi, H. B., Dubale, H. N., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.662686 · Cited by 54 · see citing works
- Authors
- Gianni, T., & Campadelli-Fiume, G.
- Affiliations
- University of Bologna (IT)
- Department of Experimental Pathology, Section on Microbiology and Virology, Alma Mater Studiorum—University of Bologna, Bologna, Italy
- ORCID
- Gianni, Tatiana
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2012-03
- Volume
- 86
- Issue
- 5
- Pages
- 2850-2855
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC3302258
- OpenAlex
- W2066108558
- Cited by
- 51
- References
- 1
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 5 · 2015: 5 · 2014: 8 · 2013: 8 · 2012: 4
- FWCI
- 4.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (submittedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Herpesvirus Infections and Treatments
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Epidemiology › Cytomegalovirus and herpesvirus research
- Keywords
- herpes simplex virus, integrin αvβ3, nectin-1, lipid rafts, viral entry, macropinocytosis, Na+/H+ exchanger
- MeSH terms
- Nectins, Cell Line, Herpes Simplex, Humans, Cell Adhesion Molecules, Herpesvirus 1, Human, Protein Transport, Membrane Microdomains, Integrin alphaVbeta3, Virus Internalization
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