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4FQH

Crystal Structure of Fab CR9114

Summary for 4FQH
Entry DOI10.2210/pdb4fqh/pdb
Related4FNK 4FQI 4FQJ 4FQK 4FQL 4FQM 4FQV 4FQY
Descriptorantibody CR9114 heavy chain, antibody CR9114 light chain, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsneutralizing antibodies, antibody affinity, antigens, epitope, glycosylation, hemagglutinin glycoproteins, immunoglobulin fab fragment, influenza virus, influenza vaccines, membrane fusion, immune system
Biological sourceHomo sapiens (human)
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Total number of polymer chains4
Total formula weight95085.21
Authors
Dreyfus, C.,Wilson, I.A. (deposition date: 2012-06-25, release date: 2012-08-22, Last modification date: 2018-01-31)
Primary citationDreyfus, 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: 22878502
DOI: 10.1126/science.1222908
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

226707

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