EMD-23780
BG505 SOSIP MD39 in complex with the monoclonal antibodies Rh.33104 mAb.1 and RM20A3
EMD-23780
Single-particle3.3 Å
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Map released: 26/01/2022
Last modified: 06/11/2024
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
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
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From structure to sequence: Antibody discovery using cryoEM.
Antanasijevic A
,
Bowman CA
,
Kirchdoerfer RN
,
Cottrell CA
,
Ozorowski G
,
Upadhyay AA
,
Cirelli KM,
Carnathan DG,
Enemuo CA,
Sewall LM,
Nogal B
,
Zhao F
,
Groschel B
,
Schief WR
,
Sok D
,
Silvestri G
,
Crotty S
,
Bosinger SE
,
Ward AB
(2022) Sci Adv , 8 , eabk2039 - eabk2039
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(2022) Sci Adv , 8 , eabk2039 - eabk2039
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.
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.