Expression or subcellular targeting of virus capsid proteins with cloning genome of a canine parvovirus from China

A strain of canine parvovirus (CPV), designated B2004, was isolated from the stool of a sick dog in Beijing. The partial genome (4623 bp) was cloned, sequenced with sequence showing B2004 to be a member of the widely distributed CPV-2a subclade. A completed VP2 or 11-residue N-terminal peptide (MAPPAKRARRG) of VP1 from B2004 was also tested for its ability to mediate nuclear transport of a heterologous protein, in this case enhanced green fluorescence protein (EGFP). EGFP was detected in the nucleus when it fused with the VP1 peptide; it was distributed primarily in the nucleus and also in the cytoplasm either when it fused with VP2, or in the cytoplasm when expressed on its own. In common with other parvoviruses the CPV VP1 N-terminal peptide contributes to the nuclear localization of the gene product.