Characterization of a reduced peptide bond analogue of a promiscuous CD4 T cell epitope derived from the Plasmodium falciparum malaria vaccine candidate merozoite surface protein 1

Molecular Immunology
Max BastianClaudia A Daubenberger

Abstract

Use of synthetic peptides as vaccine components is hampered by their susceptibility to enzymatic degradation and rapid clearance from biological fluids. Introduction of non-natural structural modifications can render peptides more resistant to enzymatic degradation, encouraging attempts to profile such non-natural ligands as components of synthetic sub-unit vaccines. We have compared the antigenic and immunogenic properties of a series of non-natural peptide analogues derived from a promiscuous T cell epitope of the major Plasmodium falciparum malaria vaccine candidate merozoite surface protein 1 (MSP-1). A series of HLA class II restricted MSP-1(38-58)-specific TCC established from three volunteers were characterized for their minimal epitope and fine specificity. T cell stimulatory activities of a series of pseudo-peptide analogues with single reduced peptide bond Psi-[CH2-NH] modifications were compared with those of single d-amino acid replacement analogues. Compared to reduced peptide bond analogues the single d-amino acid replacement analogues turned out to be less suitable for stimulation of TCC. In particular, the reduced peptide analogue carrying a Psi-[CH2-NH] backbone modification between positions V52 and L53 of MSP...Continue Reading

Citations

Feb 22, 2011·Expert Review of Vaccines·Nathan P Croft, Anthony W Purcell
Apr 1, 2008·Expert Opinion on Drug Discovery·Claudia A DaubenbergerNicole Westerfeld
Jun 26, 2012·Journal of Autoimmunity·Nicolas SchallSylviane Muller
Dec 13, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Hernando CurtidorManuel E Patarroyo
Dec 8, 2010·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·José Manuel LozanoManuel Elkin Patarroyo
Aug 9, 2019·The Journal of Immunology : Official Journal of the American Association of Immunologists·Ross W ChelohaHidde L Ploegh

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