7MDT
BG505 SOSIP.v5.2 in complex with the monoclonal antibody Rh4O9.8 (as Fab fragment)
Summary for 7MDT
Entry DOI | 10.2210/pdb7mdt/pdb |
EMDB information | 23778 23779 |
Descriptor | Surface protein gp120, Transmembrane protein gp41, Rh4O9.8 monoclonal antibody Light Chain, ... (8 entities in total) |
Functional Keywords | monoclonal antibody, polyclonal antibody, immune complex, viral protein |
Biological source | Human immunodeficiency virus 1 More |
Total number of polymer chains | 8 |
Total formula weight | 265419.15 |
Authors | Antanasijevic, A.,Ozorowski, G.,Nogal, B.,Ward, A.B. (deposition date: 2021-04-06, release date: 2022-01-26, Last modification date: 2024-11-06) |
Primary citation | Antanasijevic, A.,Bowman, C.A.,Kirchdoerfer, R.N.,Cottrell, C.A.,Ozorowski, G.,Upadhyay, A.A.,Cirelli, K.M.,Carnathan, D.G.,Enemuo, C.A.,Sewall, L.M.,Nogal, B.,Zhao, F.,Groschel, B.,Schief, W.R.,Sok, D.,Silvestri, G.,Crotty, S.,Bosinger, S.E.,Ward, A.B. From structure to sequence: Antibody discovery using cryoEM. Sci Adv, 8:eabk2039-eabk2039, 2022 Cited by PubMed Abstract: One of the rate-limiting steps in analyzing immune responses to vaccines or infections is the isolation and characterization of monoclonal antibodies. Here, we present a hybrid structural and bioinformatic approach to directly assign the heavy and light chains, identify complementarity-determining regions, and discover sequences from cryoEM density maps of serum-derived polyclonal antibodies bound to an antigen. When combined with next-generation sequencing of immune repertoires, we were able to specifically identify clonal family members, synthesize the monoclonal antibodies, and confirm that they interact with the antigen in a manner equivalent to the corresponding polyclonal antibodies. This structure-based approach for identification of monoclonal antibodies from polyclonal sera opens new avenues for analysis of immune responses and iterative vaccine design. PubMed: 35044813DOI: 10.1126/sciadv.abk2039 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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