EMD-23780

Single-particle
3.3 Å
EMD-23780 Deposition: 06/04/2021
Map released: 26/01/2022
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-23780

BG505 SOSIP MD39 in complex with the monoclonal antibodies Rh.33104 mAb.1 and RM20A3

EMD-23780

Single-particle
3.3 Å
EMD-23780 Deposition: 06/04/2021
Map released: 26/01/2022
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Macaca mulatta, Human immunodeficiency virus 1
Sample: BG505 SOSIP MD39 in complex with the monoclonal antibodies Rh.33104 mAb.1 and RM20A3
Fitted models: 7mdu (Avg. Q-score: 0.517)

Deposition Authors: Antanasijevic A , Ward AB
From structure to sequence: Antibody discovery using cryoEM.
PUBMED: 35044813
DOI: doi:10.1126/sciadv.abk2039
ISSN: 2375-2548
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.