Marek's disease virus phosphorylated polypeptide pp38 alters transcription rates of mitochondrial electron transport and oxidative phosphorylation genes.

Two splice variants of the Marek's disease virus phosphorylated polypeptide (pp)38 were previously identified in the quail cell line QTP32 expressing pp38 under the control of an inducible promoter. We developed QT35-derived cell lines expressing these splice variants or full length pp38 with the splice acceptor sites mutated to further elucidate the role of pp38. Only induction of full length pp38 resulted in an increase in mitochondrial succinate dehydrogenase activity compared to non-induced cells. Transcript copy numbers of cytochrome C oxidase subunit I and ATP synthase were reduced in induced cells. The ATP content of isolated mitochondria from induced cells was greatly reduced compared to those of non-induced cells. Mitochondrial and pp38 staining suggests that there is no direct interaction between pp38 and the mitochondria. Mitochondrial transcripts were also reduced in DF-1 cells expressing full length pp38 and in MDV-infected chick kidney cells indicating that this effect occurs independent of other viral genes and after in vitro infection with MDV.