PMID: 8960114Aug 1, 1996Paper

Reproducing the immune response against the Plasmodium vivax merozoite surface protein 1 with mimotopes selected from a phage-displayed peptide library

Molecular Immunology
C DemangelJ C Mazie

Abstract

We have used phage display technology to identify peptides binding D14-3, a monoclonal antibody raised against the M(r) 42,000 C-terminal fragment of Plasmodium vivax merozoite surface protein 1 (PvMSP1). By screening a constrained hexapeptide library, seven independent clones binding D14-3 were isolated. The reactivity of D14-3 for these peptides was lower than for the natural antigen and the antibody binding was strictly associated with the viral context and the peptide conformation. Sequence analysis showed that five of them shared homology with the M(r) 42,000 C-terminal fragment (Pv42) and therefore appears to identify the D14-3 epitope. However, the other two peptides, while related to each other, did not correspond to any sequence in the Pv42 molecules. To evaluate their immunological interest, these phagotopes were injected into mice belonging to Balb/c, IC57BI/6 and Biozzi strains. All animals developed a strong immune response against phage particles but only Biozzi mice produced antibodies cross-reacting with Pv42. All phagotopes in Biozzi mice elicited a specific response against Pv42, even those sharing no sequence similarity with the antigen. Moreover, the avidities of these immune sera and the polyclonal response...Continue Reading

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Citations

Oct 29, 1998·Protein Science : a Publication of the Protein Society·A NandiS S Visweswariah
Oct 11, 2003·Biotechnology Advances·I Benhar
Jul 27, 1999·Combinatorial Chemistry & High Throughput Screening·G CesareniG Cestra
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Jun 26, 2012·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Tengfei LiPierre Lafaye
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Dec 4, 2004·The Journal of Allergy and Clinical Immunology·Brigitte HantuschErika Jensen-Jarolim

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