4FQV
Crystal structure of broadly neutralizing antibody CR9114 bound to H7 influenza hemagglutinin
Summary for 4FQV
Entry DOI | 10.2210/pdb4fqv/pdb |
Related | 4FNK 4FQH 4FQI 4FQJ 4FQK 4FQL 4FQM 4FQY |
Descriptor | Hemagglutinin HA1, Hemagglutinin HA2, Antibody CR9114 heavy chain, ... (4 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 |
Cellular location | Host apical cell membrane ; Single-pass type I membrane protein : Q6VMK1 Q6VMK1 |
Total number of polymer chains | 12 |
Total formula weight | 307968.69 |
Authors | Ekiert, D.C.,Dreyfus, C.,Wilson, I.A. (deposition date: 2012-06-25, release date: 2012-08-22, Last modification date: 2024-11-27) |
Primary citation | Dreyfus, C.,Laursen, N.S.,Kwaks, T.,Zuijdgeest, D.,Khayat, R.,Ekiert, D.C.,Lee, J.H.,Metlagel, Z.,Bujny, M.V.,Jongeneelen, M.,van der Vlugt, R.,Lamrani, M.,Korse, H.J.,Geelen, E.,Sahin, O.,Sieuwerts, M.,Brakenhoff, J.P.,Vogels, R.,Li, O.T.,Poon, L.L.,Peiris, M.,Koudstaal, W.,Ward, A.B.,Wilson, I.A.,Goudsmit, J.,Friesen, R.H. Highly conserved protective epitopes on influenza B viruses. Science, 337:1343-1348, 2012 Cited by PubMed Abstract: Identification of broadly neutralizing antibodies against influenza A viruses has raised hopes for the development of monoclonal antibody-based immunotherapy and "universal" vaccines for influenza. However, a substantial part of the annual flu burden is caused by two cocirculating, antigenically distinct lineages of influenza B viruses. Here, we report human monoclonal antibodies, CR8033, CR8071, and CR9114, that protect mice against lethal challenge from both lineages. Antibodies CR8033 and CR8071 recognize distinct conserved epitopes in the head region of the influenza B hemagglutinin (HA), whereas CR9114 binds a conserved epitope in the HA stem and protects against lethal challenge with influenza A and B viruses. These antibodies may inform on development of monoclonal antibody-based treatments and a universal flu vaccine for all influenza A and B viruses. PubMed: 22878502DOI: 10.1126/science.1222908 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (5.75 Å) |
Structure validation
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