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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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Rigidity Emerges during Antibody Evolution in Three Distinct Antibody Systems: Evidence from QSFR Analysis of Fab
Tong Li1, Malgorzata B Tracka2, Shahid Uddin2
1Department of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, North Carolina, United States of America.
Plos Computational Biology
|July 2, 2015
Summary
Somatic mutations alter antibody flexibility during affinity maturation. The Distance Constraint Model reveals specific domain and loop rigidification/flexibilization crucial for antibody function.
Area of Science:
- Immunology
- Structural Biology
- Computational Biology
Background:
- Somatic hypermutation refines antibody specificity and affinity.
- Understanding conformational changes during affinity maturation is key to antibody engineering.
Purpose of the Study:
- To compare the effects of somatic mutations on antibody conformational flexibility.
- To investigate how germline (GL) antibodies transform into affinity mature (AM) antibodies.
Main Methods:
- Utilized the Distance Constraint Model (DCM), a statistical mechanical approach.
- Combined DCM with molecular dynamics (MD) simulations.
- Analyzed three germline-affinity mature antibody fragment (Fab) pairs.
Main Results:
- Affinity maturation led to VH domain rigidification and VL domain/CDR L2 loop flexibilization.
- CDR H3 loop rigidity increased, consistent with prior research.
- Conformational flexibility redistribution was mainly driven by H-bond network changes.
Conclusions:
- Antibody affinity maturation involves a complex interplay of domain and loop flexibility/rigidity changes.
- These alterations are critical for achieving high-affinity, monospecific antibodies.
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