{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T21:41:19Z","timestamp":1790286079094,"version":"4.1.0"},"reference-count":23,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2024,2,14]],"date-time":"2024-02-14T00:00:00Z","timestamp":1707868800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2024,2,14]],"date-time":"2024-02-14T00:00:00Z","timestamp":1707868800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100005895","name":"Fred Hutchinson Cancer Center","doi-asserted-by":"crossref","award":["Diverse Trainee Fund"],"award-info":[{"award-number":["Diverse Trainee Fund"]}],"id":[{"id":"10.13039\/100005895","id-type":"DOI","asserted-by":"crossref"}]},{"name":"HHS | National Institutes of Health","award":["Diseases of Public Health Importance Training Grant 2T32AI007509"],"award-info":[{"award-number":["Diseases of Public Health Importance Training Grant 2T32AI007509"]}]},{"name":"HHS | National Institutes of Health","award":["Viral Pathogenesis and Evolution Training Grant T32 AI083203"],"award-info":[{"award-number":["Viral Pathogenesis and Evolution Training Grant T32 AI083203"]}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2024,2,14]]},"abstract":"<jats:p>Antibodies that potently cross-neutralize Zika (ZIKV) and dengue (DENV) viruses are attractive to induce via vaccination to protect against these co-circulating flaviviruses. Structural studies have shown that viral envelope protein glycosylation is important for binding by one class of these so-called broadly neutralizing antibodies, but less is known about its effect on neutralization. Here, we investigated how envelope protein glycosylation site mutations impact the potency of broadly neutralizing antibodies against ZIKV and DENV. We found that glycan occupancy was not always predicted by an intact N-X-S\/T sequence motif. Moreover, envelope protein glycosylation site mutations alter the potency of broadly neutralizing antibodies in a manner unexpected from their predicted binding mechanism as determined by existing structures. We therefore highlight the complex role and determinants of envelope protein glycosylation that should be considered in the design of vaccine antigens to elicit broadly neutralizing antibodies.<\/jats:p>","DOI":"10.1128\/mbio.03048-23","type":"journal-article","created":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T14:01:13Z","timestamp":1704808873000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":12,"title":["Defining the impact of flavivirus envelope protein glycosylation site mutations on sensitivity to broadly neutralizing antibodies"],"prefix":"10.1128","volume":"15","author":[{"given":"Maya","family":"Contreras","sequence":"first","affiliation":[{"name":"Vaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jackson B.","family":"Stuart","sequence":"additional","affiliation":[{"name":"Vaccine and 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