5GJT

Crystal structure of H1 hemagglutinin from A/Washington/05/2011 in complex with a neutralizing antibody 3E1

Summary for 5GJT

• Entry DOI: 10.2210/pdb5gjt/pdb
• Related: 5GJS
• Descriptor: Hemagglutinin, light chain of human neutralizing antibody 3E1, heavy chain of human neutralizing antibody 3E1, ... (5 entities in total)
• Functional Keywords: epitope, fab, complementarity determining region, paratope, immune system
• Biological source: Influenza A virus; More
• Total number of polymer chains: 4
• Total formula weight: 104947.49

Authors

Wang, W.,Zhang, T.,Ding, J. (deposition date: 2016-07-01, release date: 2016-12-07, Last modification date: 2024-10-16)

Primary citation

Wang, W.,Sun, X.,Li, Y.,Su, J.,Ling, Z.,Zhang, T.,Wang, F.,Zhang, H.,Chen, H.,Ding, J.,Sun, B.
Human antibody 3E1 targets the HA stem region of H1N1 and H5N6 influenza A viruses
Nat Commun, 7:13577-13577, 2016

PubMed Abstract: As influenza A viruses remain a major threat to human health worldwide, the discovery of broadly neutralizing monoclonal antibodies that recognize conserved epitopes would facilitate the development of antibody-based therapeutic strategies. Here we report that a V4-4-encoded human mAb named 3E1 could neutralize H1 and H5 subtype viruses in vitro and protect mice against the H1N1 and H5N6 viruses by inhibiting the low pH-induced conformational rearrangement of haemagglutinin (HA), hence blocking membrane fusion. The crystal structures of 3E1 Fab in complex with HA of two H1N1 strains reveal that 3E1, with both heavy and light chains, binds to a conserved epitope of the HA stem region, comprising parts of the fusion peptide, the F subdomain and the outermost β-strand preceding helix A. Altogether, these data suggest the potential of 3E1 as a therapeutic drug against H1 and H5 subtype viruses.

PubMed: 27910950
DOI: 10.1038/ncomms13577

Experimental method

X-RAY DIFFRACTION (3.1 Å)