ABSTRACT
Little is known about the non-structural protein 6(NSP6)of rotavirus.This report describes expression of the NSP6 of a group A human rotavirus strain TB-Chen in bacteria,and its immunological properties and cellular distribution.The results showed that the recombinant NSP6(rNSP6)was expressed in high efficiency without any other proteins fused(possesses about 34.2% of total bacterial proteins).rNSP6 elicited mono-specific antibodies in immunized guinea pigs and the antibodies could react with the rNSP6 itself and the viral NSP6 proteins synthesized in SA11-or Wa-infected MA104 cells in Western blot and immunofluorescence assay.The NSP6 distributed evenly in the cytoplasm mainly around the nucleus of virus-infected cells,no viroplasm-like gathering observed;The top amount of NSP6 synthesized in SA11-infected cells or Wa-infected cells could be detected at 12h after infection.This is the first report about the high expression of entire NSP6(without any other proteins fused)in prokaryotic expression system and detection of NSP6 synthesis in virus infected cells by immunofluorescence assay.The results are important to understand the structure,biological properties and further application of the NSP6.