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

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Date
2004
Author
Alaba, Martha Patricia
Salazar, Luz Mary
Purmova, Jindra
Vanegas, MagnoliaAutoridad Universidad de Rosario
Rodriguez, Raul
Patarroyo, Manuel Elkin
Métricas

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

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."

Keyword

Peptide ; Malaria ; SERA ; NMR ;

Source link

https://www.sciencedirect.com/science/article/pii/S0264410X03006819...

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