ArticleScientific reports2015
Structural basis for epitope masking and strain specificity of a conserved epitope in an intrinsically disordered malaria vaccine candidate.
Article in Scientific reports, 2015. 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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13 citing papers in PubMed.
- Detergent-free isolation and characterization of amyloid precursor protein C99 in E. coli native lipid-nanodiscs using non-ionic polymer.Protein science : a publication of the Protein Society · 2025Article
- Nanodisc Reconstitution and Characterization of Amyloid-β Precursor Protein C99.Analytical chemistry · 2024Article
- Nanodisc reconstitution and characterization of amyloid-β precursor protein C99.bioRxiv : the preprint server for biology · 2024Article
- Naturally acquired IgG responses toFrontiers in immunology · 2024Article
- FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins.Nucleic acids research · 2023Article
- Comprehending B-Cell Epitope Prediction to Develop Vaccines and Immunodiagnostics.Frontiers in immunology · 2022Article
- Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018Review
- Proteome-wide mapping of immune features onto Plasmodium protein three-dimensional structures.Scientific reports · 2018Article
- Transient antibody-antigen interactions mediate the strain-specific recognition of a conserved malaria epitope.Communications biology · 2018Article
- FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies.Nucleic acids research · 2017Article
- Applications of (19)F-NMR in Fragment-Based Drug Discovery.Molecules (Basel, Switzerland) · 2016Review
- Strain-transcending immune response generated by chimeras of the malaria vaccine candidate merozoite surface protein 2.Scientific reports · 2016Article
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10 authors.
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Abstract
Merozoite surface protein 2 (MSP2) is an intrinsically disordered, membrane-anchored antigen of the malaria parasite Plasmodium falciparum. MSP2 can elicit a protective, albeit strain-specific, antibody response in humans. Antibodies are generated to the conserved N- and C-terminal regions but many of these react poorly with the native antigen on the parasite surface. Here we demonstrate that recognition of a conserved N-terminal epitope by mAb 6D8 is incompatible with the membrane-bound conformation of that region, suggesting a mechanism by which native MSP2 escapes antibody recognition. Furthermore, crystal structures and NMR spectroscopy identify transient, strain-specific interactions between the 6D8 antibody and regions of MSP2 beyond the conserved epitope. These interactions account for the differential affinity of 6D8 for the two allelic families of MSP2, even though 6D8 binds to a fully conserved epitope. These results highlight unappreciated mechanisms that may modulate the specificity and efficacy of immune responses towards disordered antigens.
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