Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348842
Type: Artigo
Title: Plasmodium vivax apical membrane antigen-1: comparative recognition of different domains by antibodies induced during natural human infection
Author: Mufalo, Bruno C.
Gentil, Fernanda
Bargieri, Daniel Y.
Costa, Fabio T. M.
Rodrigues, Mauricio M.
Soares, Irene S.
Abstract: The Apical Membrane Antigen-1 (AMA-1) of Plasmodium sp. has been suggested as a vaccine candidate against malaria. This protein seems to be involved in merozoite invasion and its extra-cellular portion contains three distinct domains: DI, DII, and DIII. Previously, we described that Plasmodium vivax AMA-1 (PvAMA-1) ectodomain is highly immunogenic in natural human infections. Here, we expressed each domain, separately or in combination (DI-II or DII-III), as bacterial recombinant proteins to map immunodominant epitopes within the PvAMA-1 ectodomain. IgG recognition was assessed by ELISA using sera of P. vivax-infected individuals collected from endemic regions of Brazil or antibodies raised in immunized mice. The frequencies of responders to recombinant proteins containing the DII were higher than the others and similar to the ones observed against the PvAMA-1 ectodomain. Moreover, ELISA inhibition assays using the PvAMA-1 ectodomain as substrate revealed the presence of many common epitopes within DI-II that are recognized by human immune antibodies. Finally, immunization of mice with the PvAMA-1 ectodomain induced high levels of antibodies predominantly to DI-II. Together, our results indicate that DII is particularly immunogenic during natural human infections, thus indicating that this region could be used as part of an experimental sub-unit vaccine to prevent vivax malaria
Subject: Malaria
Plasmodium vivax
Country: França
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.micinf.2008.07.023
Address: https://europepmc.org/article/med/18692152
Date Issue: 2008
Appears in Collections:IB - Artigos e Outros Documentos

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