Antigenic Repeat Structures in Proteins ofPlasmodium Falciparum
- 28 September 2007
- book chapter
- Published by Wiley
- Vol. 119, 164-183
- https://doi.org/10.1002/9780470513286.ch10
Abstract
The majority of malaria antigens that have been cloned contain short sequence repeats which encode antigenic epitopes that are naturally immunogenic. Synthetic peptides have been used to show that natural antibody responses to a strain-specific Plasmodium falciparum S antigen are largely directed against epitopes encoded in an 11-amino acid sequence that is repeated approximately 100 times in the molecule. A 16-amino acid peptide conjugated to bovine serum albumin induced antibodies specific for the S antigen of the homologous isolate. Synthetic peptides have also been used to confirm the natural immunogenicity of epitopes encoded within two blocks of related repeats in the Ring-infected Erythrocyte Surface Antigen (RESA). A 16-amino acid peptide, comprising four repeats of the tetrameric sequence EENV, induced antibodies reactive with the native molecule. Detailed analyses of these anti-peptide antisera indicate that short sequence repeats express more than one epitope, some of which may cross-react with other repeat structures.Keywords
This publication has 28 references indexed in Scilit:
- Localization of the ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum in merozoites and ring-infected erythrocytes.The Journal of Experimental Medicine, 1985
- The molecular evolution of the immune responseImmunology Today, 1985
- Antibodies in malarial sera to parasite antigens in the membrane of erythrocytes infected with early asexual stages of Plasmodium falciparum.The Journal of Experimental Medicine, 1984
- Isolate-specific S-antigen of Plasmodium falciparum contains a repeated sequence of eleven amino acidsNature, 1983
- Identification and chemical synthesis of a tandemly repeated immunogenic region of Plasmodium knowlesi circumsporozoite proteinNature, 1983
- Peptide synthesis. Part 3. Comparative solid-phase syntheses of human β-endorphin on polyamide supports using t-butoxycarbonyl and fluorenylmethoxycarbonyl protecting groupsJournal of the Chemical Society, Perkin Transactions 1, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Serotyping Plasmodium falciparum malaria with S-antigensNature, 1980
- ANTIGEN RECOGNITION AND THE IMMUNE RESPONSEThe Journal of Experimental Medicine, 1972
- Solid Phase Peptide Synthesis. I. The Synthesis of a TetrapeptideJournal of the American Chemical Society, 1963