Single-Virus Force Spectroscopy Discriminates the Intrinsic Role of Two Viral Glycoproteins upon Cell Surface Attachment
| Autor: | Martin Delguste, Florian Cotin, David Alsteens, Laurent Gillet, Grégoire Le Brun, Bénédicte Machiels |
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| Přispěvatelé: | UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology |
| Rok vydání: | 2020 |
| Předmět: |
viruses
Cell Bioengineering 02 engineering and technology Virus Cell Line Glycosaminoglycan Viral Envelope Proteins medicine Humans General Materials Science Gene Glycoproteins chemistry.chemical_classification Glycosaminoglycan binding biology Spectrum Analysis Mechanical Engineering Murid herpesvirus 4 Force spectroscopy General Chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics biology.organism_classification Cell biology medicine.anatomical_structure chemistry Viruses 0210 nano-technology Glycoprotein |
| Zdroj: | Nano Letters, Vol. 21, no. 1, p. 847-853 (2021) |
| ISSN: | 1530-6992 1530-6984 |
| DOI: | 10.1021/acs.nanolett.0c04609 |
| Popis: | Viruses are one of the most efficient pathogenic entities on earth, resulting from millions of years of evolution. Each virus particle carries the minimum number of genes and proteins to ensure their reproduction within host cells, hijacking some host replication machinery. However, the role of some viral proteins is not yet unraveled, with some appearing even redundant. For example, murid herpesvirus 4, the current model for human gammaherpesvirus infection, can bind to cell surface glycosaminoglycans using both glycoproteins gp70 and gH/gL. Here, using atomic force microscopy, we discriminate their relative contribution during virus binding to cell surface glycosaminoglycans. Single-virus force spectroscopy experiments demonstrate that gH/gL is the main actor in glycosaminoglycan binding, engaging more numerous and more stable interactions. We also demonstrated that Fab antibody fragments targeting gH/gL or gp70 appear to be a promising treatment to prevent the attachment of virions to cell surfaces. |
| Databáze: | OpenAIRE |
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