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.
Edson
C M
CM
Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002478:Cells, Cultured; D003001:Cloning, Molecular; D005347:Fibroblasts; D014645:Herpesvirus 3, Human / Q000378:metabolism*; D006801:Humans; D007231:Infant, Newborn; D008297:Male; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D012867:Skin; D013431:Sulfates / Q000378:metabolism*; D013462:Sulfur Radioisotopes; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis; D014759:Viral Envelope Proteins / Q000096:biosynthesis*
D009838:Oligodeoxyribonucleotides; D013431:Sulfates; D013462:Sulfur Radioisotopes; D014759:Viral Envelope Proteins; C056913:glycoprotein E, varicella-zoster virus; C005662:tyrosine O-sulfate; D014443:Tyrosine