Open AccessDephosphorylation of eIF2α Mediated by the γ 1 34.5 Protein of Herpes Simplex Virus 1 Facilitates Viral Neuroinvasion
Author(s) -
Dustin Verpooten,
Zongdi Feng,
Tibor Vályi-Nagy,
Yijie Ma,
Huali Jin,
Zhipeng Yan,
Cuizhu Zhang,
Youjia Cao,
Bin He
Publication year - 2009
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01431-09
Subject(s) - biology , dephosphorylation , herpes simplex virus , virology , viral replication , virulence , protein phosphatase 1 , phosphorylation , virulence factor , protein subunit , viral protein , virus , viral structural protein , phosphatase , protein phosphatase 2 , viral entry , gene , microbiology and biotechnology , biochemistry
The γ1 34.5 protein, a virulence factor of herpes simplex viruses, redirects protein phosphatase 1 to dephosphorylate the α subunit of translation initiation factor 2 (eIF2α). Additionally, it inhibits the induction of antiviral genes by TANK-binding kinase 1. Nevertheless, its precise role in vivo remains to be established. Here we show that eIF2α dephosphorylation by γ1 34.5 is crucial for viral neuroinvasion. V193 E and F195 L substitutions in γ1 34.5 abrogate viral replication in the eye and spread to the trigeminal ganglia and brain. Intriguingly, inhibition of antiviral gene induction by γ1 34.5 is not sufficient to exhibit viral virulence.