Abstract
The aim of this study was to evaluate the contribution of positively charged amino acid residues for the Uukuniemi virus (UUKV) N protein functionality. Based on phlebovirus nucleocapsid (N) protein alignments and 3D-structure predictions of UUKV N protein, 14 positively charged residues were chosen as targets for the mutagenesis. The impact of mutations to the N protein functionality was analyzed using minigenome-, virus-like particle-, and mammalian two-hybrid-assays. Seven of the mutations affected the functional competence in all three assays, while others had milder impact or no impact at all. In the 3D-model of UUKV N protein, five of the affected residues, R61, R64, R73, R98 and R115, were located either within or in close proximity to the central cavity that could potentially bind RNA.
Original language | English (US) |
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Pages (from-to) | 118-123 |
Number of pages | 6 |
Journal | Virus Research |
Volume | 167 |
Issue number | 1 |
DOIs | |
State | Published - Jul 2012 |
Keywords
- Mutational analysis
- Negative-strand RNA virus
- Nucleocapsid protein
- Oligomerization
- Phlebovirus
- RNA binding
- Uukuniemi virus
ASJC Scopus subject areas
- Virology
- Infectious Diseases
- Cancer Research