[Purification and identification of the bovine rotavirus receptor on MA104 cells]

In this research the bovine rotavirus(BRV) receptor on MA104 cells was purified and identified. The monoclonal antibody(McAb) against BRV receptor was coupled with the CNBr-activited sepharose 4B. BRV receptor was purified from the MA104 cell extracts by the method of the immunoaffinity chromatography. The results of the indirect ELISA ard the dot immunobinding assay showed that the BRV receptor antigenicity of the purified compound was positive. On SDS-polyacrylamide gel electrophoresis (SDS-PAGE) the eluate from the column with the McAb coupled showed a single band, corresponding to the elution peak. The eluate from the column without antibody showed no such a band on SDS-PAGE. The result of Western blot showed the purified compound could be distinguished by the McAb against BRV receptor. Solid-phase assay showed the purified compound had the ability to bind BRV. The mouse immunoserum against the purified compound could block the BRV infection to its host cells. The experimental results above showed that the purified compound was the receptor for BRV.