ArticleThe Journal of biological chemistry2012
Protein dynamics and the diversity of an antibody response.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift.The Biochemical journal · 2020Article
- Probing the Kinetic and Thermodynamic Fingerprints of Anti-EGF Nanobodies by Surface Plasmon Resonance.Pharmaceuticals (Basel, Switzerland) · 2020Article
- Computational Design of an Allosteric Antibody Switch by Deletion and Rescue of a Complex Structural Constellation.ACS central science · 2020Article
- T-Cell Receptor Variable β Domains Rigidify During Affinity Maturation.Scientific reports · 2020Article
- Local and Global Rigidification Upon Antibody Affinity Maturation.Frontiers in molecular biosciences · 2020Article
- Structure and Dynamics of Stacking Interactions in an Antibody Binding Site.Biochemistry · 2019Article
- Conformational Plasticity in Broadly Neutralizing HIV-1 Antibodies Triggers Polyreactivity.Cell reports · 2018Article
- Characterizing the Diversity of the CDR-H3 Loop Conformational Ensembles in Relationship to Antibody Binding Properties.Frontiers in immunology · 2018Article
- Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification.Frontiers in immunology · 2018Article
- Somatic Mutations Modulate Autoantibodies against Galactose-Deficient IgA1 in IgA Nephropathy.Journal of the American Society of Nephrology : JASN · 2016Article
- Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies.Structure (London, England : 1993) · 2016Article
- Probing the Impact of Local Structural Dynamics of Conformational Epitopes on Antibody Recognition.Biochemistry · 2016Article
- Targeting Stereotyped B Cell Receptors from Chronic Lymphocytic Leukemia Patients with Synthetic Antigen Surrogates.The Journal of biological chemistry · 2016Article
- Antibody Binding Modulates Conformational Exchange in Domain III of Dengue Virus E Protein.Journal of virology · 2016Article
- Adaptive mutations alter antibody structure and dynamics during affinity maturation.Biochemistry · 2015Article
- Thermodynamic mechanism for the evasion of antibody neutralization in flaviviruses.Journal of the American Chemical Society · 2014Article
- Effective harmonic potentials: insights into the internal cooperativity and sequence-specificity of protein dynamics.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The immune system is remarkable in its ability to produce antibodies (Abs) with virtually any specificity from a limited repertoire of germ line precursors. Although the contribution of sequence diversity to this molecular recognition has been studied for decades, recent models suggest that protein dynamics may also broaden the range of targets recognized. To characterize the contribution of protein dynamics to immunological molecular recognition, we report the sequence, thermodynamic, and time-resolved spectroscopic characterization of a panel of eight Abs elicited to the chromophoric antigen 8-methoxypyrene-1,3,6-trisulfonate (MPTS). Based on the sequence data, three of the Abs arose from unique germ line Abs, whereas the remaining five comprise two sets of siblings that arose by somatic mutation of a common precursor. The thermodynamic data indicate that the Abs recognize MPTS via a variety of mechanisms. Although the spectroscopic data reveal small differences in protein dynamics, the anti-MPTS Abs generally show similar levels of flexibility and conformational heterogeneity, possibly representing the convergent evolution of the dynamics necessary for function. However, one Ab is significantly more rigid and conformationally homogeneous than the others, including a sibling Ab from which it differs by only five somatic mutations. This example of divergent evolution demonstrates that point mutations are capable of fixing significant differences in protein dynamics. The results provide unique insight into how high affinity Abs may be produced that bind virtually any target and possibly, from a more general perspective, how new protein functions are evolved.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.