6CJK
Anti HIV Fab 10A
Summary for 6CJK
| Entry DOI | 10.2210/pdb6cjk/pdb |
| Descriptor | Immunoglobulin Fab light chain, Immunoglobulin Fab heavy chain, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | fab, hiv, immune system |
| Biological source | Oryctolagus cuniculus (rabbit) More |
| Total number of polymer chains | 4 |
| Total formula weight | 93096.46 |
| Authors | Hangartner, L.,Ward, A.B.,Wilson, I.A.,Oyen, D. (deposition date: 2018-02-26, release date: 2018-08-15, Last modification date: 2024-11-06) |
| Primary citation | Bianchi, M.,Turner, H.L.,Nogal, B.,Cottrell, C.A.,Oyen, D.,Pauthner, M.,Bastidas, R.,Nedellec, R.,McCoy, L.E.,Wilson, I.A.,Burton, D.R.,Ward, A.B.,Hangartner, L. Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization. Immunity, 49:288-300.e8, 2018 Cited by PubMed Abstract: Characterizing polyclonal antibody responses via currently available methods is inherently complex and difficult. Mapping epitopes in an immune response is typically incomplete, which creates a barrier to fully understanding the humoral response to antigens and hinders rational vaccine design efforts. Here, we describe a method of characterizing polyclonal responses by using electron microscopy, and we applied this method to the immunization of rabbits with an HIV-1 envelope glycoprotein vaccine candidate, BG505 SOSIP.664. We detected known epitopes within the polyclonal sera and revealed how antibody responses evolved during the prime-boosting strategy to ultimately result in a neutralizing antibody response. We uncovered previously unidentified epitopes, including an epitope proximal to one recognized by human broadly neutralizing antibodies as well as potentially distracting non-neutralizing epitopes. Our method provides an efficient and semiquantitative map of epitopes that are targeted in a polyclonal antibody response and should be of widespread utility in vaccine and infection studies. PubMed: 30097292DOI: 10.1016/j.immuni.2018.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.795 Å) |
Structure validation
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