ArticleJournal of the American Society for Mass Spectrometry2017
Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Epitope Mapping of Japanese Encephalitis Virus Neutralizing Antibodies by Native Mass Spectrometry and Hydrogen/Deuterium Exchange.Biomolecules · 2024Article
- Structure-guided design of VAR2CSA-based immunogens and a cocktail strategy for a placental malaria vaccine.PLoS pathogens · 2024Article
- Collision Induced Unfolding Enables the Quantitation of Isomass Biotherapeutics in Complex Biological Matrices.Journal of the American Society for Mass Spectrometry · 2023Article
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Comparing Selected-Ion Collision Induced Unfolding with All Ion Unfolding Methods for Comprehensive Protein Conformational Characterization.Journal of the American Society for Mass Spectrometry · 2022Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Glycoproteomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021Article
- Mapping a Conformational Epitope of Hemagglutinin A Using Native Mass Spectrometry and Ultraviolet Photodissociation.Analytical chemistry · 2020Article
- VHH characterization. Comparison of recombinant with chemically synthesized anti-HER2 VHH.Protein science : a publication of the Protein Society · 2019Article
- Article
- Quantitative collision-induced unfolding differentiates model antibody-drug conjugates.Protein science : a publication of the Protein Society · 2019Article
- Evolution of Structural Biology through the Lens of Mass Spectrometry.Analytical chemistry · 2019Review
- Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding.Analytical chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Plasmodium vivax Duffy Binding Protein (PvDBP) is a promising vaccine candidate for P. vivax malaria. Recently, we reported the epitopes on PvDBP region II (PvDBP-II) for three inhibitory monoclonal antibodies (2D10, 2H2, and 2C6). In this communication, we describe the combination of native mass spectrometry and ion mobility (IM) with collision induced unfolding (CIU) to study the conformation and stabilities of three malarial antigen-antibody complexes. These complexes, when collisionally activated, undergo conformational changes that depend on the location of the epitope. CIU patterns for PvDBP-II in complex with antibody 2D10 and 2H2 are highly similar, indicating comparable binding topology and stability. A different CIU fingerprint is observed for PvDBP-II/2C6, indicating that 2C6 binds to PvDBP-II on an epitope different from 2D10 and 2H2. This work supports the use of CIU as a means of classifying antigen-antibody complexes by their epitope maps in a high throughput screening workflow. Graphical Abstract ᅟ.
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