EXPRESSION AND PURIFICATION OF RECOMBINANT MAREKS-DISEASE VIRUS SEROTYPE-1 SPECIFIC PHOSPHORYLATED PROTEIN-PP38 IN ESCHERICHIA-COLI

Phosphorylated protein pp38 is the only protein that is detected in the Marek's disease (MD) lymphoma caused by MD virus serotype 1 (MDV-1) and lymphoblastoid cell lines. In this study, a recombinant protein coded for by the almost entire open reading frame of the MDV-1 pp38 cDNA was produced in E. coli and purified by affinity chromatography. Prior to the expression and purification of the protein, cDNA containing the entire coding region for pp38 was cloned and its nucleotide sequence was determined. Immunoblot analysis indicated that the expressed recombinant protein electrophoresed close to that of the pp38 in infected cells. The difference in mobility of the purified recombinant and the pp38 in infected cells corresponded to a fusion peptide. The recombinant pp38 may be of interest for function analyses and the diagnotic use of pp38.