The P gene of human parainfluenza virus type 3 (HPIV 3) encodes a multicistronic P mRNA that gives rise to four polypeptides. The P and C proteins are synthesized from two discrete overlapping AUG codons from the unedited P mRNA, while synthesis of two additional proteins, V and PD, presumably occurs via a unique transcriptional editing mechanism. However, the presence of V and PD proteins in HPIV 3 infected cells and their role in viral replication remains uncertain. Here, in vitro expression of full-length PD protein from an altered P mRNA and generation of a polyclonal antibody to the COOH-terminus of PD was achieved. Confocal immunofluorescence analysis following Leptomycin B (LMB) treatment revealed the presence of PD protein in nuclear and cytoplasmic compartments of HPIV 3 infected cells suggesting the involvement of a nuclear localization signal in this process. These initial results provide new impetus for further characterization of the role of PD in HPIV 3 infection.