Homotypic interaction of Bunyamwera virus nucleocapsid protein.
The bunyavirus nucleocapsid protein, N, plays a central role in viral replication in encapsidating the three genomic RNA segments to form functional templates for transcription and replication by the viral RNA-dependent RNA polymerase. Here we report functional mapping of interacting domains of the Bunyamwera orthobunyavirus N protein by yeast and mammalian two-hybrid systems, immunoprecipitation experiments, and chemical cross-linking studies. N forms a range of multimers from dimers to high-molecular-weight structures, independently of the presence of RNA. Deletion of the N- or C-terminal domains resulted in loss of activity in a minireplicon assay and a decreased capacity for N to form higher multimers. Our data suggest a head-to-head and tail-to-tail multimerization model for the orthobunyavirus N protein.[1]References
- Homotypic interaction of Bunyamwera virus nucleocapsid protein. Leonard, V.H., Kohl, A., Osborne, J.C., McLees, A., Elliott, R.M. J. Virol. (2005) [Pubmed]
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