Structurally convergent antibodies derived from different vaccine strategies target the influenza virus HA anchor epitope with a subset of VH3 and VK3 genes

Ting-Hui Lin, Chang-Chun David Lee, Monica L. Fernández-Quintero, James A. Ferguson, Julianna Han, Xueyong Zhu, Wenli Yu, Jenna J. Guthmiller, Florian Krammer, Patrick C. Wilson, Andrew B. Ward () and Ian A. Wilson ()
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Ting-Hui Lin: The Scripps Research Institute
Chang-Chun David Lee: The Scripps Research Institute
Monica L. Fernández-Quintero: The Scripps Research Institute
James A. Ferguson: The Scripps Research Institute
Julianna Han: The Scripps Research Institute
Xueyong Zhu: The Scripps Research Institute
Wenli Yu: The Scripps Research Institute
Jenna J. Guthmiller: University of Colorado Anschutz Medical Campus
Florian Krammer: Icahn School of Medicine at Mount Sinai
Patrick C. Wilson: Weill Cornell Medicine
Andrew B. Ward: The Scripps Research Institute
Ian A. Wilson: The Scripps Research Institute

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract H1N1 influenza viruses are responsible for both seasonal and pandemic influenza. The continual antigenic shift and drift of these viruses highlight the urgent need for a universal influenza vaccine to elicit broadly neutralizing antibodies (bnAbs). Identification and characterization of bnAbs elicited in natural infection and immunization to influenza virus hemagglutinin (HA) can provide insights for development of a universal influenza vaccine. Here, we structurally and biophysically characterize four antibodies that bind to a conserved region on the HA membrane-proximal region known as the anchor epitope. Despite some diversity in their VH and VK genes, the antibodies interact with the HA through germline-encoded residues in HCDR2 and LCDR3. Somatic mutations on HCDR3 also contribute hydrophobic interactions with the conserved HA epitope. This convergent binding mode provides extensive neutralization breadth against H1N1 viruses and suggests possible countermeasures against H1N1 viruses.

Date: 2025
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DOI: 10.1038/s41467-025-56496-4

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