9AZV

CH67 Fab bound to A/Massachusetts/1/1990 influenza hemagglutinin head with a G189E mutation (2)

9AZV の概要

• エントリーDOI: 10.2210/pdb9azv/pdb
• 分子名称: CH67 Fab heavy chain, CH67 Fab light chain, Hemagglutinin HA1 chain, ... (4 entities in total)
• 機能のキーワード: antibody, influenza, hemagglutinin, uca, antiviral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 75499.79

構造登録者

Maurer, D.P.,Schmidt, A.G. (登録日: 2024-03-11, 公開日: 2025-03-12, 最終更新日: 2025-03-19)

主引用文献

Maurer, D.P.,Vu, M.,Schmidt, A.G.
Antigenic drift expands influenza viral escape pathways from recalled humoral immunity.
Immunity, 58:716-727.e6, 2025

PubMed Abstract: Initial exposure to a rapidly evolving virus establishes B cell memory that biases later responses to antigenically drifted strains. This "immune imprinting" implies that subsequent exposure to a drifted strain can induce affinity maturation of memory B cells toward cross-reactivity with the drifted strain and hence toward greater overall breadth. Here, we used deep mutational scanning of H1 influenza hemagglutinins (HAs) to investigate how viruses evolve in response to these broad antibody response. We identified escape mutations from clonal antibody lineages that targeted the receptor binding site and lateral patch. By adjusting the antigen-antibody contacts, antibody affinity maturation restricted the potential escape routes for the eliciting strain. However, escape occurred readily in drifted strains. We attribute this escape-prone property of the drifted strains to epistatic networks within HA. Our data explain how the influenza virus continues to evolve in the human population by escaping even broad antibody responses.

PubMed: 40023162
DOI: 10.1016/j.immuni.2025.02.006

実験手法

X-RAY DIFFRACTION (3.16 Å)