Andrea DiCarlo

Philipps University of Marburg, Marburg, Hesse, Germany

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Publications (2)7.87 Total impact

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    ABSTRACT: Phosphorylation of the Marburg virus nucleoprotein NP is distributed over 7 regions (I-VII) in its C-terminus. The exact localization of phosphorylated amino acids and function of NP phosphorylation are unknown. Here, we show that the major phosphate acceptor sites in NP region II are serine 446 and serines 453-455; the latter are located in a cluster of 6 serine residues (aa 450-455). The function of phosphorylation in region II was tested using an infectious virus-like particle assay. Phosphorylation influenced reporter gene activity that reflects viral transcription and replication. An NP mutant mimicking 3 phosphorylated serine residues at position 453-455 supported reporter gene activity better than wild-type NP. Negative charges at positions 450-452 and when the serine cluster was completely substituted by alanine inhibited reporter gene activity significantly. These data support the idea that phosphorylation of NP region II modulates viral RNA synthesis in transcription and/or replication.
    The Journal of Infectious Diseases 11/2011; 204 Suppl 3:S927-33. DOI:10.1093/infdis/jir319 · 5.78 Impact Factor
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    ABSTRACT: The nucleoprotein (NP) of Marburg virus (MARV) is responsible for the encapsidation of viral genomic RNA and the formation of the helical nucleocapsid precursors that accumulate in intracellular inclusions in infected cells. To form the large helical MARV nucleocapsid, NP needs to interact with itself and the viral proteins VP30, VP35 and L, which are also part of the MARV nucleocapsid. In the present study, a conserved coiled coil motif in the central part of MARV NP was shown to be an important element for the interactions of NP with itself and VP35, the viral polymerase cofactor. Additionally, the coiled coil motif was essential for the formation of NP-induced intracellular inclusions and for the function of NP in the process of transcription and replication of viral RNA in a minigenome system. Transfer of the coiled coil motif to a reporter protein was sufficient to mediate interaction of the constructed fusion protein with the N-terminus of NP. The coiled coil motif is bipartite, constituted by two coiled coils which are separated by a flexible linker.
    Virology Journal 02/2007; 4(1):105. DOI:10.1186/1743-422X-4-105 · 2.09 Impact Factor

Publication Stats

14 Citations
7.87 Total Impact Points

Institutions

  • 2007–2011
    • Philipps University of Marburg
      • Institut für Virologie
      Marburg, Hesse, Germany