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.
Leonard
Vincent H J
VH
Division of Virology, Institute of Biomedical and Life Sciences, University of Glasgow, Scotland, UK.
Kohl
Alain
A
Osborne
Jane C
JC
McLees
Angela
A
Elliott
Richard M
RM
D002042:Bunyamwera virus / Q000235:genetics / Q000502:physiology*; D008970:Molecular Weight; D019251:Nucleocapsid / Q000737:chemistry / Q000378:metabolism*; D019590:Nucleocapsid Proteins; D017434:Protein Structure, Tertiary / Q000502:physiology; D012367:RNA, Viral / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
C423924:N protein, Bunyamwera bunyavirus; D019590:Nucleocapsid Proteins; D012367:RNA, Viral