IMPORTANCE OF LEUCINE ZIPPER-LIKE DOMAIN OF RIFT VALLEY FEVER VIRUS L PROTEIN FOR VIRAL RNA SYNTHESIS

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Rift Valley fever virus (RVFV) (genus Phlebovirus, family Bunyaviridae) causes mosquito-borne endemic and epidemic diseases among humans and livestock. The virus carries three RNA segments, L, M and S. The L RNA encodes L protein, an RNA-dependent RNA polymerase and a RVFV L oligomer, together with N, which is encoded by the S RNA, exerts viral RNA synthesis. Although RVFV L encodes conserved domains among other segmented RNA viruses, the functional domains of RVFV L have not yet been characterized. The N-terminus region of L contained a leucine zipper-like domain, in which leucine residues repeat 4 times at every 7th position. By mutational analysis combined with minigenome assay, Co-immunoprecipitation or Bi-molecular Fluorescence assay (BiFC), we demonstrated that the leucine zipper-like domain was important for intramolecular interaction with C-terminus to exert viral RNA synthesis.