3SDY

Crystal Structure of Broadly Neutralizing Antibody CR8020 Bound to the Influenza A H3 Hemagglutinin

Summary for 3SDY

• Entry DOI: 10.2210/pdb3sdy/pdb
• Descriptor: Hemagglutinin HA1 chain, SULFATE ION, Hemagglutinin HA2 chain, ... (10 entities in total)
• Functional Keywords: viral fusion protein, immunoglobulin, virus attachment and entry, immune recognition, viral protein-immune system complex, viral protein/immune system
• Biological source: Influenza A virus; More
• Total number of polymer chains: 4
• Total formula weight: 108301.75

Authors

Ekiert, D.C.,Wilson, I.A. (deposition date: 2011-06-09, release date: 2011-07-20, Last modification date: 2021-04-07)

Primary citation

Ekiert, D.C.,Friesen, R.H.,Bhabha, G.,Kwaks, T.,Jongeneelen, M.,Yu, W.,Ophorst, C.,Cox, F.,Korse, H.J.,Brandenburg, B.,Vogels, R.,Brakenhoff, J.P.,Kompier, R.,Koldijk, M.H.,Cornelissen, L.A.,Poon, L.L.,Peiris, M.,Koudstaal, W.,Wilson, I.A.,Goudsmit, J.
A highly conserved neutralizing epitope on group 2 influenza A viruses.
Science, 333:843-850, 2011

PubMed Abstract: Current flu vaccines provide only limited coverage against seasonal strains of influenza viruses. The identification of V(H)1-69 antibodies that broadly neutralize almost all influenza A group 1 viruses constituted a breakthrough in the influenza field. Here, we report the isolation and characterization of a human monoclonal antibody CR8020 with broad neutralizing activity against most group 2 viruses, including H3N2 and H7N7, which cause severe human infection. The crystal structure of Fab CR8020 with the 1968 pandemic H3 hemagglutinin (HA) reveals a highly conserved epitope in the HA stalk distinct from the epitope recognized by the V(H)1-69 group 1 antibodies. Thus, a cocktail of two antibodies may be sufficient to neutralize most influenza A subtypes and, hence, enable development of a universal flu vaccine and broad-spectrum antibody therapies.

PubMed: 21737702
DOI: 10.1126/science.1204839

Experimental method

X-RAY DIFFRACTION (2.85 Å)