RT Journal Article SR Electronic(1) A1 Wolff, Thorsten A1 Pfleger, Rene A1 Wehner, Tatjana A1 Reinhardt, Jens A1 Richt, Juergen A. YR 2000 T1 A short leucine-rich sequence in the Borna disease virus p10 protein mediates association with the viral phospho- and nucleoproteins JF Journal of General Virology, VO 81 IS 4 SP 939 OP 947 DO https://doi.org/10.1099/0022-1317-81-4-939 PB Microbiology Society, SN 1465-2099, AB Borna disease virus (BDV) is unique among the non-segmented negative-strand RNA viruses of animals and man because it transcribes and replicates its genome in the nucleus of the infected cell. It has recently been discovered that BDV expresses a gene product of 87 amino acids, the p10 protein, from an open reading frame that overlaps with the gene encoding the viral p24 phosphoprotein. In addition, the p10 protein has been localized to intranuclear BDV-specific clusters containing viral antigens. Here, characterization of p10 interactions with the viral nucleoprotein p38/p39 and the p24 phosphoprotein is reported. Immunoaffinity chromatography demonstrated the presence of high-salt stable complexes of p10 containing the p24 and p38/p39 proteins in extracts of BDV-infected cells. Analyses in the yeast two-hybrid system and biochemical co-precipitation experiments suggested that the p10 protein binds directly to the p24 phosphoprotein and indirectly to the viral nucleoprotein. Mutational analysis demonstrated that a leucine-rich stretch of amino acids at positions 8–15 within the p10 protein is critical for interaction with p24. Furthermore, binding of p10 to the viral phosphoprotein was shown to be important for association with the BDV-specific intranuclear clusters that may represent the sites of virus replication and transcription in infected cells. These findings are discussed with respect to possible roles for the p10 protein in viral RNA synthesis or ribonucleoprotein transport., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-81-4-939