Tyrosine sulfation of varicella-zoster virus envelope glycoprotein gpl.

Abstract:

: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.

journal_name

Virology

journal_title

Virology

authors

Edson CM

doi

10.1006/viro.1993.1576

subject

Has Abstract

pub_date

1993-11-01 00:00:00

pages

159-65

issue

1

eissn

0042-6822

issn

1096-0341

pii

S004268228371576X

journal_volume

197

pub_type

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