8GHK

CryoEM structure of Influenza A virus A/Melbourner/1/1946 (H1N1) hemagglutinin bound to GS10-X6-BE4 Fab

Summary for 8GHK

• Entry DOI: 10.2210/pdb8ghk/pdb
• EMDB information: 40046
• Descriptor: Hemagglutinin, GS10-X6-BE4 Fab Heavy chain, GS10-X6-BE4 Fab light chain, ... (6 entities in total)
• Functional Keywords: niaid, hemagglutinin stalk binding antibody, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Influenza A virus; More
• Total number of polymer chains: 7
• Total formula weight: 225778.86

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2023-03-10, release date: 2024-06-26, Last modification date: 2024-10-23)

Primary citation

Nagashima, 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

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

Experimental method

ELECTRON MICROSCOPY (3.47 Å)