Antigenic repeat structures in proteins of Plasmodium falciparum

R. F. Anders, P. T. Shi, D. B. Scanlon, S. J. Leach, R. L. Coppel, G. V. Brown, H. D. Stahl, D. J. Kemp

Research output: Contribution to journalReview ArticleResearchpeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)164-183
Number of pages20
JournalCiba Foundation Symposium
Publication statusPublished - 1 Jan 1986

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