6N5E
Broadly protective antibodies directed to a subdominant influenza hemagglutinin epitope
Summary for 6N5E
| Entry DOI | 10.2210/pdb6n5e/pdb |
| Descriptor | Hemagglutinin, FL-1066 heavy chain, FL-1066 light chain, ... (4 entities in total) |
| Functional Keywords | influenza, antibody, complex, hemagglutinin, immunogen design, glycan, viral protein-immune system complex, viral protein/immune system |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 9 |
| Total formula weight | 241306.45 |
| Authors | Bajic, G.,Schmidt, A.G. (deposition date: 2018-11-21, release date: 2019-06-05, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 31104946DOI: 10.1016/j.chom.2019.04.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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