6DID
HIV Env BG505 SOSIP with polyclonal Fabs from immunized rabbit #3417 post-boost#1
Summary for 6DID
| Entry DOI | 10.2210/pdb6did/pdb |
| EMDB information | 7896 |
| Descriptor | Envelope glycoprotein gp160, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total) |
| Functional Keywords | hiv, antibodies, antibody, viral protein |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 12 |
| Total formula weight | 378243.01 |
| Authors | Turner, H.L.,Cottrell, C.A.,Oyen, D.,Wilson, I.A.,Ward, A.B. (deposition date: 2018-05-23, release date: 2018-09-05, Last modification date: 2024-11-20) |
| 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 | ELECTRON MICROSCOPY (4.71 Å) |
Structure validation
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