Induction and displacement of an helix in the 6725 SERA peptide analogue confers protection against P. falciparum malaria.

Magnolia Vanegas Murcia, Martha Patricia Alba, Luz Mary Salazar, Jindra Purmova, Raul Rodriguez, Manuel Elkin Patarroyo

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The protein called serine repeat antigen (SERA) is a Plasmodium falciparum malaria antigen; high activity erythrocyte binding peptides have been identified in this protein. One of these, the 6725 peptide (non-immunogenic and non-protective), was analyzed for immunogenicity and protective activity in Aotus monkeys, together with several of its analogues. These peptides were studied by NMR to try to correlate their structure with their biological function. These peptides showed helical regions having differences in their position, except for randomly structured 6725. It is shown that replacing some amino acids induced immunogenicity and protectivity against experimental malaria and changed their three-dimensional (3D) structure, suggesting that such modifications may allow a better fit with immune system molecules.
Original languageEnglish (US)
Pages (from-to)1281 - 1289
Number of pages8
JournalVaccine
Volume22
Issue number9-10
StatePublished - 2004

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