3GBN

Crystal Structure of Fab CR6261 in Complex with the 1918 H1N1 influenza virus hemagglutinin

Summary for 3GBN

• Entry DOI: 10.2210/pdb3gbn/pdb
• Related: 3GBM
• Descriptor: Hemagglutinin, CHLORIDE ION, UNKNOWN LIGAND, ... (12 entities in total)
• Functional Keywords: hemagglutinin, fab, neutralizing antibodies, antibody, pandemic flu, cell membrane, envelope protein, fusion protein, glycoprotein, lipoprotein, membrane, palmitate, transmembrane, virion, viral protein-immune system complex, viral protein/immune system
• Biological source: Influenza A virus (A/Brevig Mission/1/1918(H1N1)) (Influenza A virus (strain A/South Carolina/1/1918 H1N1)); More
• Cellular location: Virion membrane; Single-pass type I membrane protein (Potential): Q9WFX3 Q9WFX3
• Total number of polymer chains: 4
• Total formula weight: 105897.36

Authors

Ekiert, D.C.,Elsliger, M.A.,Wilson, I.A. (deposition date: 2009-02-20, release date: 2009-03-10, Last modification date: 2023-09-06)

Primary citation

Ekiert, D.C.,Bhabha, G.,Elsliger, M.A.,Friesen, R.H.,Jongeneelen, M.,Throsby, M.,Goudsmit, J.,Wilson, I.A.
Antibody recognition of a highly conserved influenza virus epitope.
Science, 324:246-251, 2009

PubMed Abstract: Influenza virus presents an important and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Cocrystal structures were determined at 2.2 and 2.7 angstrom resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1 and HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.

PubMed: 19251591
DOI: 10.1126/science.1171491

Experimental method

X-RAY DIFFRACTION (2.2 Å)