Biophysical characterization of nucleophosmin Interactions with human immunodeficiency virus rev and herpes simplex virus US11

K. Nouri, J. M. Moll, L.G. Milroy, A. Hain, R. Dvorsky, E. Amin, M. Lenders, L. Nagel-Steger, S. Howe, S. H. J. Smits, H. Hengel, L. Schmitt, C. Münk, L. Brunsveld, M. R. Ahmadian

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Abstract

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.

Original languageEnglish
Article numbere0143634
JournalPLoS ONE
Volume10
Issue number12
DOIs
Publication statusPublished - 1 Dec 2015

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