ArticlemAbs
Suppressing allostery in epitope mapping experiments using millisecond hydrogen / deuterium exchange mass spectrometry.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- HDX-MS Detects Steric Protection and Trimeric Compaction of TNFα after It Binds Receptors or Antibodies.ACS omega · 2026Article
- Structural and epitope characterization of anti-DEFA5 monoclonal antibodies clones 1A8 and 4F5 for inflammatory bowel disease subtype diagnostics.International journal of biological macromolecules · 2025Article
- HDXRank: A Deep Learning Framework for Ranking Protein Complex Predictions with Hydrogen-Deuterium Exchange Data.Journal of chemical theory and computation · 2025Article
- RosettaHDX: Predicting antibody-antigen interaction from hydrogen-deuterium exchange mass spectrometry data.Journal of structural biology · 2025Article
- Identification ofFrontiers in immunology · 2025Article
- Quantitative Hydrogen-Deuterium Exchange Mass Spectrometry for Simultaneous Structural Characterization and Affinity Indexing of Single Target Drug Candidate Libraries.Analytical chemistry · 2024Article
- Recent Progress in Antibody Epitope Prediction.Antibodies (Basel, Switzerland) · 2023Review
- Online Fully Automated System for Hydrogen/Deuterium-Exchange Mass Spectrometry with Millisecond Time Resolution.Analytical chemistry · 2023Article
- Apparatus for Automated Continuous Hydrogen Deuterium Exchange Mass Spectrometry Measurements from Milliseconds to Hours.Analytical chemistry · 2023Article
- Hydrogen Deuterium Exchange and other Mass Spectrometry-based Approaches for Epitope Mapping.Frontiers in analytical science · 2023Article
- Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.Current opinion in structural biology · 2022Review
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Computational Structure Prediction for Antibody-Antigen Complexes From Hydrogen-Deuterium Exchange Mass Spectrometry: Challenges and Outlook.Frontiers in immunology · 2022Review
- Fenton-Chemistry-Based Oxidative Modification of Proteins Reflects Their Conformation.International journal of molecular sciences · 2021Article
- Research advances in hydrogen-deuterium exchange mass spectrometry for protein epitope mapping.Analytical and bioanalytical chemistry · 2021Review
- Hydrogen-deuterium exchange mass spectrometry identifies spatially distinct antibody epitopes on domain III of the Zika virus envelope protein.Journal of mass spectrometry : JMS · 2021Article
- Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry.Protein science : a publication of the Protein Society · 2020Review
- Structural Aspects of the Allergen-Antibody Interaction.Frontiers in immunology · 2020Review
- Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification.Frontiers in immunology · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Localization of the interface between the candidate antibody and its antigen target, commonly known as epitope mapping, is a critical component of the development of therapeutic monoclonal antibodies. With the recent availability of commercial automated systems, hydrogen / deuterium eXchange (HDX) is rapidly becoming the tool for mapping epitopes preferred by researchers in both industry and academia. However, this approach has a significant drawback in that it can be confounded by 'allosteric' structural and dynamic changes that result from the interaction, but occur far from the point(s) of contact. Here, we introduce a 'kinetic' millisecond HDX workflow that suppresses allosteric effects in epitope mapping experiments. The approach employs a previously introduced microfluidic apparatus that enables millisecond HDX labeling times with on-chip pepsin digestion and electrospray ionization. The 'kinetic' workflow also differs from conventional HDX-based epitope mapping in that the antibody is introduced to the antigen at the onset of HDX labeling. Using myoglobin / anti-myoglobin as a model system, we demonstrate that at short 'kinetic' workflow labeling times (i.e., 200 ms), the HDX signal is already fully developed at the 'true' epitope, but is still largely below the significance threshold at allosteric sites. Identification of the 'true' epitope is supported by computational docking predictions and allostery modeling using the rigidity transmission allostery algorithm.
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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.