4N9G
Crystal Structure of a Computationally Designed RSV-Presenting Epitope Scaffold And Its Elicited Antibody 17HD9
Summary for 4N9G
| Entry DOI | 10.2210/pdb4n9g/pdb |
| Descriptor | Antibody 17HD9, Heavy Chain, Antibody 17HD9, Light Chain, Epitope Scaffold rsv_1isea_FFL_001_C, ... (4 entities in total) |
| Functional Keywords | antibody, hairpin, epitope scaffold, immune system |
| Biological source | Macaca mulatta More |
| Total number of polymer chains | 12 |
| Total formula weight | 249699.92 |
| Authors | Carrico, C.T.D.,Strong, R.K. (deposition date: 2013-10-21, release date: 2014-02-12, Last modification date: 2024-10-16) |
| Primary citation | Correia, B.E.,Bates, J.T.,Loomis, R.J.,Baneyx, G.,Carrico, C.,Jardine, J.G.,Rupert, P.,Correnti, C.,Kalyuzhniy, O.,Vittal, V.,Connell, M.J.,Stevens, E.,Schroeter, A.,Chen, M.,Macpherson, S.,Serra, A.M.,Adachi, Y.,Holmes, M.A.,Li, Y.,Klevit, R.E.,Graham, B.S.,Wyatt, R.T.,Baker, D.,Strong, R.K.,Crowe, J.E.,Johnson, P.R.,Schief, W.R. Proof of principle for epitope-focused vaccine design. Nature, 507:201-206, 2014 Cited by PubMed Abstract: Vaccines prevent infectious disease largely by inducing protective neutralizing antibodies against vulnerable epitopes. Several major pathogens have resisted traditional vaccine development, although vulnerable epitopes targeted by neutralizing antibodies have been identified for several such cases. Hence, new vaccine design methods to induce epitope-specific neutralizing antibodies are needed. Here we show, with a neutralization epitope from respiratory syncytial virus, that computational protein design can generate small, thermally and conformationally stable protein scaffolds that accurately mimic the viral epitope structure and induce potent neutralizing antibodies. These scaffolds represent promising leads for the research and development of a human respiratory syncytial virus vaccine needed to protect infants, young children and the elderly. More generally, the results provide proof of principle for epitope-focused and scaffold-based vaccine design, and encourage the evaluation and further development of these strategies for a variety of other vaccine targets, including antigenically highly variable pathogens such as human immunodeficiency virus and influenza. PubMed: 24499818DOI: 10.1038/nature12966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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