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

Alaba, Martha Patricia; Salazar, Luz Mary; Purmova, Jindra; Vanegas, Magnolia; Rodriguez, Raul; Patarroyo, Manuel Elkin

doi:https://doi.org/10.1016/j.vaccine.2003.08.046

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

https://repository.urosario.edu.co/handle/10336/27865
https://doi.org/10.1016/j.vaccine.2003.08.046

Autores

Alaba, Martha Patricia

Salazar, Luz Mary

Purmova, Jindra

Vanegas, Magnolia

Rodriguez, Raul

Patarroyo, Manuel Elkin

Fecha

2004

Editor

Elsevier

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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 1H 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.