Tyrosine sulfation of varicella-zoster virus envelope glycoprotein gpl.
Tyrosine sulfation of varicella-zoster virus envelope glycoprotein gpl.
复制标题
水痘带状疱疹病毒包膜糖蛋白 gpl 的酪氨酸硫酸化。
DOI：
10.1006/viro.1993.1576
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发表时间：
1993
期刊：
影响因子：
3.7
通讯作者：
Edson,CM
中科院分区：
文献类型：
--
作者：
Edson,CM
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 gpl 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.
