The role of amino acid electron-donor/acceptor atoms in host-cell binding peptides is associated with their 3D structure and HLA-binding capacity in sterile malarial immunity induction

► Fundamental residues located in some HABPs are associated with their 3D structure. ► Electron-donor atoms present in β-turn, random, distorted α-helix structures. ► Electron-donor atoms bound to HLA-DR53. ► Electron-acceptor atoms present in regular α-helix structure bound to HLA-DR52. Plasmodium...

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Veröffentlicht in:Biochemical and biophysical research communications 2012-01, Vol.417 (3), p.938-944
Hauptverfasser: Patarroyo, Manuel E., Almonacid, Hannia, Moreno-Vranich, Armando
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Sprache:eng
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Zusammenfassung:► Fundamental residues located in some HABPs are associated with their 3D structure. ► Electron-donor atoms present in β-turn, random, distorted α-helix structures. ► Electron-donor atoms bound to HLA-DR53. ► Electron-acceptor atoms present in regular α-helix structure bound to HLA-DR52. Plasmodium falciparum malaria continues being one of the parasitic diseases causing the highest worldwide mortality due to the parasite’s multiple evasion mechanisms, such as immunological silence. Membrane and organelle proteins are used during invasion for interactions mediated by high binding ability peptides (HABPs); these have amino acids which establish hydrogen bonds between them in some of their critical binding residues. Immunisation assays in the Aotus model using HABPs whose critical residues had been modified have revealed a conformational change thereby enabling a protection-inducing response. This has improved fitting within HLA-DRβ1∗ molecules where amino acid electron-donor atoms present in β-turn, random or distorted α-helix structures preferentially bound to HLA-DR53 molecules, whilst HABPs having amino acid electron-acceptor atoms present in regular α-helix structure bound to HLA-DR52. This data has great implications for vaccine development.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2011.12.005