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6E4X

Human antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2)

Summary for 6E4X
Entry DOI10.2210/pdb6e4x/pdb
DescriptorHemagglutinin, S5V2-29 light chain, S5V2-29 heavy chain, ... (9 entities in total)
Functional Keywordsinfluenza antibody, viral protein-immune system complex, viral protein/immune system
Biological sourceInfluenza A virus (A/Texas/50/2012(H3N2))
More
Total number of polymer chains3
Total formula weight84209.93
Authors
McCarthy, K.R.,Harrison, S.C. (deposition date: 2018-07-18, release date: 2019-05-22, Last modification date: 2024-11-06)
Primary citationWatanabe, 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: 31100267
DOI: 10.1016/j.cell.2019.03.048
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

237735

数据于2025-06-18公开中

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