{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T10:40:24Z","timestamp":1789468824262,"version":"build-2803163510"},"reference-count":55,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T00:00:00Z","timestamp":1786665600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T00:00:00Z","timestamp":1786665600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100012728","name":"Frederick National Laboratory for Cancer Research","doi-asserted-by":"publisher","award":["HHSN261200800001"],"award-info":[{"award-number":["HHSN261200800001"]}],"id":[{"id":"10.13039\/100012728","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["advanced.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Advanced Science"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Viral entry glycoproteins are often shielded from immune recognition by dense\n                    <jats:italic>N<\/jats:italic>\n                    \u2010linked glycans that limit antibody access to protein epitopes. While glycan\u2010reactive antibodies with unusual architectures have been described, how canonical Y\u2010shaped antibodies engage these glycan\u2010rich surfaces remains poorly defined. Here, we characterize two human antibodies, VRC35 and VRC36, isolated from an HIV\u20101\u2010infected donor, that recognize diverse glycosylated viral glycoproteins. Cryo\u2010electron microscopy structural analyses of these antibodies in complex with viral entry glycoproteins, including HIV\u20101 envelope, influenza hemagglutinin, SARS\u2010CoV\u20102 spike, and the Lassa virus glycoprotein complex, reveal adaptive Fab stoichiometries ranging from single\u2010Fab binding to dimeric and higher\u2010order assemblies are mediated by intra\u2010 and inter\u2010IgG interactions that\u00a0depend on local glycan organization. Dense glycan clustering on HIV\u20101 and influenza glycoproteins supports multivalent Fab assemblies and correlates with neutralization activity, whereas sparse glycan environments on SARS\u2010CoV\u20102 and Lassa virus favor weak or heterogeneous engagement without neutralization. Structural and mutational analyses further demonstrate that homotypic Fab\u2013Fab interactions stabilize multivalent engagement and contribute to neutralizing activity. Together, these findings define a structural framework in which viral glycan organization constrains antibody valency and engagement, while somatic hypermutation contributes to the acquisition of homotypic Fab\u2010Fab interactions that facilitate multivalent recognition of viral glycan shields.\n                  <\/jats:p>","DOI":"10.1002\/advs.77172","type":"journal-article","created":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T09:20:15Z","timestamp":1786699215000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Canonical Antibodies Adopt Distinct Binding Modes to Recognize Viral Glycan Shields"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9210-746X","authenticated-orcid":false,"given":"Jiaxuan","family":"Cheng","sequence":"first","affiliation":[{"name":"Vaccine Research Center National Institute of Allergy and Infectious Diseases National Institutes of Health  Bethesda Maryland 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