ArticleCommunications biology2018
Transient antibody-antigen interactions mediate the strain-specific recognition of a conserved malaria epitope.
Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Fuzzy binding model of molecular interactions between tropoelastin and integrin alphaVbeta3.Biophysical journal · 2021Article
- NMR mapping of the highly flexible regions ofJournal of biomolecular NMR · 2020Article
- Structural Biology, ASB/ABA meeting, Melbourne.Biophysical reviews · 2019Article
- Modulation of the aggregation of an amyloidogenic sequence by flanking-disordered region in the intrinsically disordered antigen merozoite surface protein 2.European biophysics journal : EBJ · 2019Article
- Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018Review
- Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data.Biophysical chemistryArticle
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transient interactions in which binding partners retain substantial conformational disorder play an essential role in regulating biological networks, challenging the expectation that specificity demands structurally defined and unambiguous molecular interactions. The monoclonal antibody 6D8 recognises a completely conserved continuous nine-residue epitope within the intrinsically disordered malaria antigen, MSP2, yet it has different affinities for the two allelic forms of this antigen. NMR chemical shift perturbations, relaxation rates and paramagnetic relaxation enhancements reveal the presence of transient interactions involving polymorphic residues immediately C-terminal to the structurally defined epitope. A combination of these experimental data with molecular dynamics simulations shows clearly that the polymorphic C-terminal extension engages in multiple transient interactions distributed across much of the accessible antibody surface. These interactions are determined more by topographical features of the antibody surface than by sequence-specific interactions. Thus, specificity arises as a consequence of subtle differences in what are highly dynamic and essentially non-specific interactions.
Identifiers
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Registered trials
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