Biophysical characterization of nucleophosmin Interactions with human immunodeficiency virus rev and herpes simplex virus US11
| Autor: | Luitgard Nagel-Steger, Sander H. J. Smits, Anika Hain, Sebastian Howe, Kazem Nouri, Carsten Münk, Mohammad Reza Ahmadian, Luc Brunsveld, Jens M. Moll, Michael H. H. Lenders, Hartmut Hengel, Lech-Gustav Milroy, Radovan Dvorsky, Ehsan Amin, Lutz Schmitt |
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| Přispěvatelé: | Chemical Biology |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular viruses Protein domain lcsh:Medicine Biology medicine.disease_cause SDG 3 – Goede gezondheid en welzijn Peptides Cyclic Virus Biophysical Phenomena Protein–protein interaction Single-stranded binding protein Viral Proteins Protein structure VP40 SDG 3 - Good Health and Well-being Chlorocebus aethiops medicine Animals Humans Protein Structure Quaternary lcsh:Science Nucleophosmin Multidisciplinary lcsh:R Nuclear Proteins RNA-Binding Proteins rev Gene Products Human Immunodeficiency Virus Virology Herpes simplex virus COS Cells biology.protein HIV-1 lcsh:Q Protein Multimerization HeLa Cells Protein Binding Research Article |
| Zdroj: | PLoS ONE, 10(12):e0143634. Public Library of Science PLoS ONE, Vol 10, Iss 12, p e0143634 (2015) PLoS ONE |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0143634 |
| Popis: | Nucleophosmin (NPM1, also known as B23, numatrin or NO38) is a pentameric RNA-binding protein with RNA and protein chaperon functions. NPM1 has increasingly emerged as a potential cellular factor that directly associates with viral proteins; however, the significance of these interactions in each case is still not clear. In this study, we have investigated the physical interaction of NPM1 with both human immunodeficiency virus type 1 (HIV-1) Rev and Herpes Simplex virus type 1 (HSV-1) US11, two functionally homologous proteins. Both viral proteins show, in mechanistically different modes, high affinity for a binding site on the N-terminal oligomerization domain of NPM1. Rev, additionally, exhibits low-affinity for the central histone-binding domain of NPM1.We also showed that the proapoptotic cyclic peptide CIGB-300 specifically binds to NPM1 oligomerization domain and blocks its association with Rev and US11. Moreover, HIV-1 virus production was significantly reduced in the cells treated with CIGB-300. Results of this study suggest that targeting NPM1 may represent a useful approach for antiviral intervention. |
| Databáze: | OpenAIRE |
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