6OL5
Structure of iglb12 Fab in complex with anti-idiotype ib3 Fab
Summary for 6OL5
| Entry DOI | 10.2210/pdb6ol5/pdb |
| Descriptor | ib3 Heavy Chain, ib3 Light Chain, iglb12 Heavy Chain, ... (9 entities in total) |
| Functional Keywords | glb12, antibody, ib3, fab, complex, anti-idiotype, immune system, hiv, broadly neutralizing |
| Biological source | Mus musculus More |
| Total number of polymer chains | 4 |
| Total formula weight | 97879.72 |
| Authors | Weidle, C.,Pancera, M. (deposition date: 2019-04-15, release date: 2019-07-24, Last modification date: 2024-10-09) |
| Primary citation | Bancroft, T.,DeBuysscher, B.L.,Weidle, C.,Schwartz, A.,Wall, A.,Gray, M.D.,Feng, J.,Steach, H.R.,Fitzpatrick, K.S.,Gewe, M.M.,Skog, P.D.,Doyle-Cooper, C.,Ota, T.,Strong, R.K.,Nemazee, D.,Pancera, M.,Stamatatos, L.,McGuire, A.T.,Taylor, J.J. Detection and activation of HIV broadly neutralizing antibody precursor B cells using anti-idiotypes. J.Exp.Med., 216:2331-2347, 2019 Cited by PubMed Abstract: Many tested vaccines fail to provide protection against disease despite the induction of antibodies that bind the pathogen of interest. In light of this, there is much interest in rationally designed subunit vaccines that direct the antibody response to protective epitopes. Here, we produced a panel of anti-idiotype antibodies able to specifically recognize the inferred germline version of the human immunodeficiency virus 1 (HIV-1) broadly neutralizing antibody b12 (iglb12). We determined the crystal structure of two anti-idiotypes in complex with iglb12 and used these anti-idiotypes to identify rare naive human B cells expressing B cell receptors with similarity to iglb12. Immunization with a multimerized version of this anti-idiotype induced the proliferation of transgenic murine B cells expressing the iglb12 heavy chain in vivo, despite the presence of deletion and anergy within this population. Together, our data indicate that anti-idiotypes are a valuable tool for the study and induction of potentially protective antibodies. PubMed: 31345930DOI: 10.1084/jem.20190164 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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