{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rawi R"],"funding":["Simons Foundation","Intramural NIH HHS","New York State Foundation for Science, Technology and Innovation","U.S. Department of Health and Human Services","Foundation for the National Institutes of Health","National Institute of Allergy and Infectious Diseases Vaccine Research Center","National Institutes of Health","Bill and Melinda Gates Foundation","Gates Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1820-1830.e4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12416542"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(11)"],"pubmed_abstract":["The N terminus of the H3 subtype of influenza virus hemagglutinin is ∼10 residues longer than the N termini of most other hemagglutinins. As conserved, exposed, and linear regions may be good vaccine targets, we investigated the vaccine utility of the extended H3-N terminus. First, we identified antibody 5E10, for which structure and binding analyses revealed recognition of the H3-N terminus. Second, we immunized mice with immunogens incorporating the H3-N terminus, boosted with hemagglutinin trimer, and isolated antibodies from immunogen-elicited B cells that bound both H3-N terminus and hemagglutinin trimer. However, hemagglutinin-complex structures of two such antibodies, 3864-6 and 3864-10, that neutralized H3-influenza strains, revealed only peripheral recognition of the hemagglutinin"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["The N terminus of H3-influenza hemagglutinin as a site-of-vulnerability to neutralizing antibody."],"pmcid":["PMC12416542"],"funding_grant_id":["SF349247","P41 GM103310","INV-029369","ZIC AI005114","GM103310","INV029369"],"pubmed_authors":["Bylund T","Morano NC","Gorman J","Lee M","Rawi R","Zhou T","Shapiro L","Wang L","Kanekiyo M","McDermott AB","Olia AS","Wang S","Harris DR","Ou L","Du H","Chen X","Prabhakaran M","Becker JE","Zhang B","Kwong PD","Charaf S","Cheung CS"],"additional_accession":[]},"is_claimable":false,"name":"The N terminus of H3-influenza hemagglutinin as a site-of-vulnerability to neutralizing antibody.","description":"The N terminus of the H3 subtype of influenza virus hemagglutinin is ∼10 residues longer than the N termini of most other hemagglutinins. As conserved, exposed, and linear regions may be good vaccine targets, we investigated the vaccine utility of the extended H3-N terminus. First, we identified antibody 5E10, for which structure and binding analyses revealed recognition of the H3-N terminus. Second, we immunized mice with immunogens incorporating the H3-N terminus, boosted with hemagglutinin trimer, and isolated antibodies from immunogen-elicited B cells that bound both H3-N terminus and hemagglutinin trimer. However, hemagglutinin-complex structures of two such antibodies, 3864-6 and 3864-10, that neutralized H3-influenza strains, revealed only peripheral recognition of the hemagglutinin","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-06T17:07:06.201Z","creation":"2026-06-02T03:12:01.198Z"},"accession":"S-EPMC12416542","cross_references":{"pubmed":["40816277"],"doi":["10.1016/j.str.2025.07.015"]}}