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8V7O

Fab fragment of human mAb #58 in complex with computationally optimized broadly reactive H1 influenza hemagglutinin X6

Summary for 8V7O
Entry DOI10.2210/pdb8v7o/pdb
EMDB information43008
DescriptorHemagglutinin, #58 heavy chain, #58 light chain (3 entities in total)
Functional Keywordscomplex, antibody, hemagglutinin, viral protein-immune system complex, viral protein/immune system
Biological sourceInfluenza A virus
More
Total number of polymer chains9
Total formula weight265033.40
Authors
Nagashima, K.A.,Mousa, J.J. (deposition date: 2023-12-04, release date: 2024-04-10, Last modification date: 2024-11-06)
Primary citationNagashima, K.A.,Dzimianski, J.V.,Yang, M.,Abendroth, J.,Sautto, G.A.,Ross, T.M.,DuBois, R.M.,Edwards, T.E.,Mousa, J.J.
Structural basis for the broad antigenicity of the computationally optimized influenza hemagglutinin X6.
Structure, 32:1079-, 2024
Cited by
PubMed Abstract: Influenza causes significant morbidity and mortality. As an alternative approach to current seasonal vaccines, the computationally optimized broadly reactive antigen (COBRA) platform has been previously applied to hemagglutinin (HA). This approach integrates wild-type HA sequences into a single immunogen to expand the breadth of accessible antibody epitopes. Adding to previous studies of H1, H3, and H5 COBRA HAs, we define the structural features of another H1 subtype COBRA, X6, that incorporates HA sequences from before and after the 2009 H1N1 influenza pandemic. We determined structures of this antigen alone and in complex with COBRA-specific as well as broadly reactive and functional antibodies, analyzing its antigenicity. We found that X6 possesses features representing both historic and recent H1 HA strains, enabling binding to both head- and stem-reactive antibodies. Overall, these data confirm the integrity of broadly reactive antibody epitopes of X6 and contribute to design efforts for a next-generation vaccine.
PubMed: 38810648
DOI: 10.1016/j.str.2024.05.001
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.57 Å)
Structure validation

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