9CQA

Structure of antibody 1G1 bound to the central conserved region of RSV G

9CQA の概要

• エントリーDOI: 10.2210/pdb9cqa/pdb
• 分子名称: Fab 1G1 Heavy Chain, Fab1G1 Light Chain, Mature secreted glycoprotein G, ... (5 entities in total)
• 機能のキーワード: antibody, respiratory syncytial virus, g glycoprotein, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 115100.03

構造登録者

Juarez, M.G.,DuBois, R.M. (登録日: 2024-07-19, 公開日: 2025-02-19, 最終更新日: 2025-04-02)

主引用文献

Juarez, M.G.,O'Rourke, S.M.,Dzimianski, J.V.,Gagnon, D.,Penunuri, G.,Serrao, V.H.B.,Corbett-Detig, R.B.,Kauvar, L.M.,DuBois, R.M.
Structures of respiratory syncytial virus G bound to broadly reactive antibodies provide insights into vaccine design.
Sci Rep, 15:8666-8666, 2025

PubMed Abstract: Respiratory syncytial virus (RSV) is a leading cause of severe lower respiratory tract disease in infants and older adults. The attachment glycoprotein (RSV G) binds to the chemokine receptor CX3CR1 to promote viral entry and modulate host immunity. Antibodies against RSV G are a known correlate of protection. Previously, several broadly reactive, high-affinity anti-RSV G human monoclonal antibodies were isolated from RSV-exposed individuals and were shown to be protective in vitro and in vivo. Here, we determined the structures of three of these antibodies in complex with RSV G and defined distinct conformational epitopes comprised of highly conserved RSV G residues. Binding competition and structural studies demonstrated that this highly conserved region displays two non-overlapping antigenic sites. Analyses of anti-RSV G antibody sequences reveal that antigenic site flexibility may promote the elicitation of diverse antibody germlines. Together, these findings provide a foundation for next-generation RSV prophylactics, and they expand concepts in vaccine design for the elicitation of germline lineage-diverse, broadly reactive, high-affinity antibodies.

PubMed: 40082629
DOI: 10.1038/s41598-025-92886-w

実験手法

X-RAY DIFFRACTION (1.74 Å)