9dsc

Publication Abstract from PubMed

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 V(H) and V(K) 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.

Structurally convergent antibodies derived from different vaccine strategies target the influenza virus HA anchor epitope with a subset of V(H)3 and V(K)3 genes.,Lin TH, Lee CD, Fernandez-Quintero ML, Ferguson JA, Han J, Zhu X, Yu W, Guthmiller JJ, Krammer F, Wilson PC, Ward AB, Wilson IA Nat Commun. 2025 Feb 2;16(1):1268. doi: 10.1038/s41467-025-56496-4. PMID:39894881^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.