Recombinant N-terminal part of bovine herpesvirus 1 ICP27 protein: its preparation, purification, and use for raising specific antiserum.

摘要

Recombinant N-terminal part of bovine herpesvirus-1 (BoHV-1) ICP27 protein fused with thioredoxin and His-tag ("the recombinant protein") expressed in Escherichia coli was purified by the Ni2+-NTA affinity chromatography and used for the preparation of antiserum by immunization of rabbits. The antiserum recognized the recombinant protein in Western blot analysis and was able to detect BoHV-1 ICP27 in the nucleoli of BoHV-1-infected MDBK cells. These results showed that such an antiserum could serve as a valuable tool in further studies of the functions of BoHV-1 ICP27. Keywords: Bovine herpesvirus 1, ICP27, recombinant protein, antiserum, immunofluorescence assay.