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Here we show in cell cultures that an N-glycan shield on the herpes simplex virus 1 (HSV-1) envelope glycoprotein B (gB) mediated evasion from neutralization and antibody-dependent cellular cytotoxicity due to pooled \u03b3-globulins derived from human blood. We also demonstrated that the presence of human \u03b3-globulins in mice and immunity to HSV-1 induced by viral infection in mice significantly reduced replication in their eyes of a mutant virus lacking the glycosylation site but had little effect on the replication of its repaired virus. These results suggest that an N-glycan shield on a specific site of HSV-1 envelope gB mediated evasion from human antibodies\n                    <jats:italic>in vivo<\/jats:italic>\n                    and from HSV-1 immunity induced by viral infection\n                    <jats:italic>in vivo<\/jats:italic>\n                    . Notably, we also found that an N-glycan shield on a specific site of HSV-1 gB was significant for HSV-1 neurovirulence and replication in the central nervous system of na\u00efve mice. Thus, we have identified a critical N-glycan shield on HSV-1 gB that has dual impacts, namely evasion from human antibodies\n                    <jats:italic>in vivo<\/jats:italic>\n                    and viral neurovirulence.\n                  <\/jats:p>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>Herpes simplex virus 1 (HSV-1) establishes lifelong latent and recurrent infections in humans. To produce recurrent infections that contribute to transmission of the virus to new human host(s), the virus must be able to evade the antibodies persisting in latently infected individuals. Here, we show that an N-glycan shield on the specific site of the envelope glycoprotein B (gB) of HSV-1 mediates evasion from pooled \u03b3-globulins derived from human blood both in cell cultures and mice. Notably, the N-glycan shield on the specific site of gB was also significant for HSV-1 neurovirulence in na\u00efve mice. Considering the clinical features of HSV-1 infection, these results suggest that the glycan shield not only facilitates recurrent HSV-1 infections in latently infected humans by evading antibodies but is also important for HSV-1 pathogenesis during the initial infection.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.00992-23","type":"journal-article","created":{"date-parts":[[2023,6,27]],"date-time":"2023-06-27T09:00:30Z","timestamp":1687856430000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":12,"title":["Dual impacts of a glycan shield on the envelope glycoprotein B of HSV-1: evasion from human antibodies\n                    <i>in vivo<\/i>\n                    and neurovirulence"],"prefix":"10.1128","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-3152-2079","authenticated-orcid":true,"given":"Ayano","family":"Fukui","sequence":"first","affiliation":[{"name":"Division of Molecular Virology, 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