Protection against experimental malaria associated with AMA‐1 peptide analogue structures

FEBS Letters

Pinto, Martha¹  Patarroyo, Manuel E¹  Cortes, Ximena¹  Salazar, Luz M¹  Torres, Libardo¹  Alba, Martha P¹  Torres, Maria H¹ 

[1] Fundación Instituto de Inmunologı́a de Colombia (FIDIC), Universidad Nacional de Colombia, Carrera 50 No. 26-00 Bogotá, Colombia

关键词: Apical membrane antigen-1 protein;    Peptide analogues;    Vaccine candidate;    Nuclear magnetic resonance;    Plasmodium falciparum;    AMA-1;    apical membrane antigen-1;    NMR;    nuclear magnetic resonance;    RBC;    red blood cell;    IFA;    indirect immunofluorescence assay;    DQF-COSY;    double quantum filtered correlation spectroscopy;    TOCSY;    total correlation spectroscopy;    NOESY;    NOE;    nuclear Overhauser effect spectroscopy or signal;   

DOI  :  10.1016/S0014-5793(02)03174-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

One Plasmodium falciparum malaria antigen is an integral membrane protein called apical membrane antigen-1. High activity binding peptides to human red blood cells have been identified in this protein. 4337 is a conserved, non-immunogenic peptide with high activity red blood cell binding and its critical residues have already been identified. Peptide analogues (with amino acids having the same mass but different charge) were generated to change their immunogenic and protective characteristics. Three analogues having positive or negative immunological results were studied by nuclear magnetic resonance. The studied peptides all had an α-helix fragment, but in different peptide regions and extensions, except for randomly structured 4337. We show that altering a few amino acids induced immunogenicity and protectivity against experimental malaria and changed their three-dimensional structure, suggesting a better fit with immune system molecules and that modified peptides having better immunological properties can be included in the design of new malaria multi-component subunit-based vaccine.

【 授权许可】

Unknown