Homotypic interaction of Bunyamwera virus nucleocapsid protein

Vincent H.J. Leonard, Alain Kohl, Jane C. Osborne, Angela McLees, Richard M. Elliott*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)13166-13172
Number of pages7
JournalJournal of Virology
Volume79
Issue number20
DOIs
Publication statusPublished - Oct 2005

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