Abstract: Rice black streaked dwarf virus (RBSDV)， a member of the genus Fijivirus， infects maize and rice plants and causes significant yield losses in Asia. RBSDV has a genome of 10 dsRNAs and encodes 12 proteins. Six of these proteins (P1， P2， P3， P4， P8 and P10) are structural components of the viral particle. There are six non\|structural proteins， P5， P6， P7\|1， P7\|2， P9\|1， and P9\|2. Among those non\|structural proteins， P5， P6 and P9\|1 have been shown to involve in viroplasm formation and P7\|1 has been identified to form the cytoplasmic tubular\|like structures that serve as a conduit for virion movement between cells. The function of P7\|2 and P9\|2 is still unknow. In this study， we utilized protein Pull\|Down assay and liquid chromatography\|tandem mass spectrometry (LC\|MS/MS) techniques to identify the proteins from rice (Oryza sativa) that interact with P7\|2. Four proteins were found to bind P7\|2 by Pull\|Down assay. Two of them are transcription\|associated proteins， one is an aminotransferase and the other one is a putative chaperonin 60 beta precursor. Using real\|time quantitative PCR， the transcript expression levels of transcription\|associated protein and putative chaperonin 60 beta precursor were up\|regulated by RBSDV infection. In contrast， the transcript expression of aminotransferase protein was suppressed by RBSDV infection.

Key words: Rice black streaked dwarf virus, P7\|2 gene, prokaryotic expression, protein interaction, real\|time fluorescence quantitative PCR