6E4X
Human antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2)
Summary for 6E4X
Entry DOI | 10.2210/pdb6e4x/pdb |
Descriptor | Hemagglutinin, S5V2-29 light chain, S5V2-29 heavy chain, ... (9 entities in total) |
Functional Keywords | influenza antibody, viral protein-immune system complex, viral protein/immune system |
Biological source | Influenza A virus (A/Texas/50/2012(H3N2)) More |
Total number of polymer chains | 3 |
Total formula weight | 84209.93 |
Authors | McCarthy, K.R.,Harrison, S.C. (deposition date: 2018-07-18, release date: 2019-05-22, Last modification date: 2024-11-06) |
Primary citation | Watanabe, A.,McCarthy, K.R.,Kuraoka, M.,Schmidt, A.G.,Adachi, Y.,Onodera, T.,Tonouchi, K.,Caradonna, T.M.,Bajic, G.,Song, S.,McGee, C.E.,Sempowski, G.D.,Feng, F.,Urick, P.,Kepler, T.B.,Takahashi, Y.,Harrison, S.C.,Kelsoe, G. Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism. Cell, 177:1124-1135.e16, 2019 Cited by PubMed Abstract: Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular "breathing" of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in "universal" flu vaccines. PubMed: 31100267DOI: 10.1016/j.cell.2019.03.048 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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