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Infection and Immunity, September 1999, p. 4679-4688, Vol. 67, No. 9
Department of
Biochemistry1 and the Cooperative
Research Centre for Diagnostic Technologies,
Received 28 December 1998/Returned for modification 18 February
1999/Accepted 16 June 1999
The ring-infected erythrocyte surface antigen (RESA) is a
dense-granule protein of Plasmodium falciparum which binds
to the cytoskeletal structure of the erythrocyte after parasite
invasion. It is currently under trial as a vaccine candidate. In an
effort to characterize further the antibody responses to this antigen, we have panned two independent libraries of random peptides expressed on the surface of filamentous phage with a monoclonal antibody (MAb
18/2) against RESA. One library consisted of a potentially constrained
17-mer peptide fused with the gpVIII phage coat protein, and the other
displayed an unconstrained 15-mer as a fusion with the minor phage coat
protein gpIII. Several rounds of biopanning resulted in enrichment from
both libraries clones that interacted specifically with MAb 18/2 in
protein-blotting and enzyme-linked immunosorbent assay experiments.
Nucleotide sequencing of the random oligonucleotide insert revealed a
common predominant motif: (S/T)AVDD. Several other clones had related
but degenerate motifs. Thus, a monoclonal antibody against a malarial
antigen can select common mimotopes from different random peptide
libraries. We envisage many uses for this technology in malaria research.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Isolation of Peptides That Mimic Epitopes on a Malarial
Antigen from Random Peptide Libraries Displayed on Phage
*
Corresponding author. Mailing address: Department of
Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia. Phone: 61-3-94792158. Fax: 61-3-9472467. E-mail:
m.foley{at}latrobe.edu.au.
Infection and Immunity, September 1999, p. 4679-4688, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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