{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T15:56:51Z","timestamp":1790783811510,"version":"4.1.0"},"reference-count":21,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2015,6,21]],"date-time":"2015-06-21T00:00:00Z","timestamp":1434844800000},"content-version":"vor","delay-in-days":20,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microbiology and Immunology"],"published-print":{"date-parts":[[2015,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:label\/><jats:p>Herpes simplex virus 1 (HSV\u20101) envelope glycoprotein H (gH) is important for viral entry into cells and nuclear egress of nucleocapsids. To clarify additional novel roles of gH during HSV\u20101 replication, host cell proteins that interact with gH were screened for by tandem affinity purification coupled with mass spectrometry\u2010based proteomics in 293T cells transiently expressing gH. This screen identified 123 host cell proteins as potential gH interactors. Of these proteins, general control nonderepressive\u20101 (GCN1), a <jats:italic>trans<\/jats:italic>\u2010acting positive effector of GCN2 kinase that regulates phosphorylation of the \u03b1 subunit of translation initiation factor 2 (eIF2\u03b1), was subsequently confirmed to interact with gH in HSV\u20101\u2010infected cells. eIF2\u03b1 phosphorylation is known to downregulate protein synthesis, and various viruses have evolved mechanisms to prevent the accumulation of phosphorylated eIF2\u03b1 in infected cells. Here, it was shown that <jats:italic>GCN1<\/jats:italic>  knockdown reduces phosphorylation of eIF2\u03b1 in HSV\u20101\u2010infected cells and that the <jats:italic>gH<\/jats:italic>\u2010null mutation increases eIF2\u03b1 in HSV\u20101\u2010infected cells, whereas <jats:italic>gH<\/jats:italic>  overexpression in the absence of other HSV\u20101 proteins reduces eIF2\u03b1 phosphorylation. These findings suggest that GCN1 can regulate eIF2\u03b1 phosphorylation in HSV\u20101\u2010infected cells and that the GCN1\u2010binding viral partner gH is necessary and sufficient to prevent the accumulation of phosphorylated eIF2\u03b1. Our database of 123 host cell proteins potentially interacting with gH will be useful for future studies aimed at unveiling further novel functions of gH and the roles of cellular proteins in HSV\u20101\u2010infected cells.<\/jats:p><\/jats:sec>","DOI":"10.1111\/1348-0421.12255","type":"journal-article","created":{"date-parts":[[2015,3,24]],"date-time":"2015-03-24T20:01:59Z","timestamp":1427227319000},"page":"331-337","source":"Crossref","is-referenced-by-count":8,"title":["Interactome analysis of herpes simplex virus 1 envelope glycoprotein H"],"prefix":"10.1111","volume":"59","author":[{"given":"Yoshitaka","family":"Hirohata","sequence":"first","affiliation":[{"name":"Division of Molecular Virology Department of Microbiology and Immunology"},{"name":"Department of Infectious Disease Control International Research Center for Infectious 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