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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
Published on: March 15, 2019
13.2K
Structural diversity in a human antibody germline library.
Alexey Teplyakov1, Galina Obmolova1, Thomas J Malia1
1a Janssen Research & Development LLC, Spring House , PA , USA.
Mabs
|May 24, 2016
Summary
Crystal structures of antibody variants reveal how heavy and light chain pairings influence complementarity-determining region (CDR) H3 conformation, crucial for antibody therapeutic development.
Area of Science:
- Structural Biology
- Immunology
- Biochemistry
Background:
- Antibody engineering is vital for therapeutic development.
- Understanding antibody structural variations is key to predicting function.
Purpose of the Study:
- Determine crystal structures of 16 germline antibody variants.
- Analyze the impact of heavy and light chain pairing on antibody structure and CDR conformation.
Main Methods:
- X-ray crystallography to determine antigen-binding fragment (Fab) structures.
- Comparative analysis of overall structures, CDR conformations, and variable domain packing.
Main Results:
- CDR conformations are generally clustered, with longer CDRs showing more diversity.
- Complementarity-determining region H3 (CDR H3) exhibits significant conformational diversity despite identical sequences.
- Heavy and light chain pairing influences CDR H3 conformation.
- Most antibody stem regions adopt a 'kinked' conformation.
Conclusions:
- Antibody CDR H3 conformation is dictated by both amino acid sequence and the surrounding structural environment.
- Structural insights from these variants can guide future antibody modeling and engineering.
- Variations in variable domain tilt angles were observed in specific pairings.
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