9DSC

Crystal structure of Apo-241_2F04-A95a mutant Fab

9DSC の概要

• エントリーDOI: 10.2210/pdb9dsc/pdb
• 分子名称: 241_2F04-A95a, Heavy chain, 241_2F04-A95a, Light chain (3 entities in total)
• 機能のキーワード: antibody, immune system
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95134.32

構造登録者

Lin, T.H.,Wilson, I.A. (登録日: 2024-09-26, 公開日: 2025-03-19)

主引用文献

Lin, T.H.,Lee, C.D.,Fernandez-Quintero, M.L.,Ferguson, J.A.,Han, J.,Zhu, X.,Yu, W.,Guthmiller, J.J.,Krammer, F.,Wilson, P.C.,Ward, A.B.,Wilson, I.A.
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.
Nat Commun, 16:1268-1268, 2025

PubMed 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 V and V 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.

PubMed: 39894881
DOI: 10.1038/s41467-025-56496-4

実験手法

X-RAY DIFFRACTION (2.01 Å)