6N5B

Broadly protective antibodies directed to a subdominant influenza hemagglutinin epitope

6N5B の概要

• エントリーDOI: 10.2210/pdb6n5b/pdb
• 分子名称: antibody heavy chain, antibody light chain, Hemagglutinin, ... (4 entities in total)
• 機能のキーワード: influenza, antibody, complex, hemagglutinin, immunogen design, glycan, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Mus musculus (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 71689.94

構造登録者

Bajic, G.,Maron, M.J.,Schmidt, A.G. (登録日: 2018-11-21, 公開日: 2019-06-05, 最終更新日: 2024-11-20)

主引用文献

Bajic, G.,Maron, M.J.,Adachi, Y.,Onodera, T.,McCarthy, K.R.,McGee, C.E.,Sempowski, G.D.,Takahashi, Y.,Kelsoe, G.,Kuraoka, M.,Schmidt, A.G.
Influenza Antigen Engineering Focuses Immune Responses to a Subdominant but Broadly Protective Viral Epitope.
Cell Host Microbe, 25:827-, 2019

PubMed Abstract: Viral glycoproteins are under constant immune surveillance by a host's adaptive immune responses. Antigenic variation including glycan introduction or removal is among the mechanisms viruses have evolved to escape host immunity. Understanding how glycosylation affects immunodominance on complex protein antigens may help decipher underlying B cell biology. To determine how B cell responses can be altered by such modifications, we engineered glycans onto the influenza virus hemagglutinin (HA) and characterized the molecular features of the elicited humoral immunity in mice. We found that glycan addition changed the initially diverse antibody repertoire into an epitope-focused, genetically restricted response. Structural analyses showed that one antibody gene family targeted a previously subdominant, occluded epitope at the head interface. Passive transfer of this antibody conferred Fc-dependent protection to influenza virus-challenged mice. These results have potential implications for next-generation viral vaccines aimed at directing B cell responses to preferred epitope(s).

PubMed: 31104946
DOI: 10.1016/j.chom.2019.04.003

実験手法

X-RAY DIFFRACTION (3.5 Å)