Tyrosine sulfation of varicella-zoster virus envelope glycoprotein gpl

Sulfation is a common post-translational modification of secreted and membrane proteins, with the sulfate attached to tyrosine residues or to glycan side-chains. I have shown that varicella-zoster virus (VZV) envelope glycoproteins gpI, gpII, and gpIII can be labeled with [35S]sulfate. The predominant VZV glycoprotein, gpI, was shown to be sulfated on asparagine-linked glycans and on tyrosine. This is the first report of tyrosine sulfation of a viral envelope glycoprotein. Examination of the predicted amino acid sequences of gpI from the Dumas and CP-5262 VZV strains revealed the presence of a single consensus sequence for tyrosine sulfation of tyr88:IWPRNDYDGFLEN. Consensus sequences are also present in the homologues of gpI in herpes simplex type 1, herpes simplex type 2, and pseudorabies virus, suggesting that tyrosine sulfation may be a general post-translational modification of the neurotropic alphaherpesviruses.