The V protein of Newcastle disease virus (NDV) is produced by the inse
rtion of a single nontemplated G residue at a specific point during tr
anscription of the phosphoprotein (P) gene, accessing a new reading fr
ame upon translation. The V protein, in common with its counterpart in
other paramyxoviruses contains a highly cysteine rich motif near the
carboxyl terminus, suggestive of a zinc-binding domain. By constructin
g E. coli overexpression plasmids for the NDV P and V proteins, and mo
nitoring the binding of (ZnCl2)-Zn-65 to proteins electroblotted onto
nitrocellulose membranes, we have demonstrated that the V protein stro
ngly binds zinc.