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The HSV\u20101 envelope contains\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylated proteins involved in infection and that are candidate drug targets. NGI\u20101 is a small\u2010molecule inhibitor of oligosaccharyltransferase (OST) complexes STT3A\u2010OST and STT3B\u2010OST, which catalyze cotranslational and post\u2010translational\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation, respectively. Because host OSTs attach HSV\u20101 glycans, NGI\u20101 might have anti\u2013HSV\u20101 activity. We evaluated HSV\u20101 function using NGI\u20101 and human embryonic kidney 293 knockout lines for OST isoform\u2010specific catalytic and accessory subunits.\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation of 2 representative envelope proteins (gC and gD) was primarily dependent upon STT3A\u2010OST, but to a large extent replaceable by STT3B\u2010OST. Knockouts impairing STT3A\u2010 or STT3B\u2010OST activity, by themselves, did not appreciably affect HSV\u20101 function (plaque\u2010forming units, normalized to viral particles measured by unglycosylated capsid protein VP5 content). However, with cells lacking STT3B\u2010OST activity (missing the catalytic subunit STT3B or the oxidoreductase subunits magnesium transporter 1\/tumor suppressor candidate 3) and thus solely dependent upon STT3A\u2010OST for\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation, NGI\u20101 treatment resulted in HSV\u20101 having cell type\u2013dependent dysfunction (affecting infectivity with Vero cells much more than with the 293 lines). Ablation of post\u2010translational\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation can therefore make HSV\u20101 infectivity, and possibly masking of immunogenic peptide epitopes by glycans, highly sensitive to pharmacological inhibition of cotranslational\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation.\u2014Lu, H., Cherepanova, N. A., Gilmore, R., Contessa, J. N., Lehrman, M. A. Targeting STT3A\u2010oligosaccharyltransferase with NGI\u20101 causes herpes simplex virus 1 dysfunction. FASEB J. 33, 6801\u20136812 (2019).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.201802044rr","type":"journal-article","created":{"date-parts":[[2019,2,27]],"date-time":"2019-02-27T16:32:06Z","timestamp":1551285126000},"page":"6801-6812","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Targeting STT3A\u2010oligosaccharyltransferase with NGI\u20101 causes herpes simplex virus 1 dysfunction"],"prefix":"10.1096","volume":"33","author":[{"given":"Hua","family":"Lu","sequence":"first","affiliation":[{"name":"Department of Pharmacology University of Texas Southwestern Medical Center Dallas Texas USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natalia A.","family":"Cherepanova","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology University of Massachusetts Medical School Worcester Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reid","family":"Gilmore","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology University of Massachusetts Medical School Worcester Massachusetts USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph N.","family":"Contessa","sequence":"additional","affiliation":[{"name":"Department of Therapeutic Radiology Yale School of Medicine New Haven Connecticut USA"},{"name":"Department of Pharmacology Yale School of Medicine New Haven Connecticut USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark A.","family":"Lehrman","sequence":"additional","affiliation":[{"name":"Department of Pharmacology University of Texas Southwestern Medical Center Dallas Texas USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2019,2,27]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1004784"},{"key":"e_1_2_9_3_1","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1128\/jvi.17.3.991-1008.1976","article-title":"Membrane proteins specified by herpes simplex viruses. 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