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Background  Technical limitations for culturing the human malaria parasite  Plasmodium vivax  have impaired the discovery of vaccine candidates, challenging the malaria eradication agenda. The immunogenicity of the M2 domain of the Merozoite Adhesive Erythrocytic Binding Protein (MAEBL) antigen cloned from the  Plasmodium yoelii  murine parasite, has been previously demonstrated.    Results  Detailed epitope mapping of MAEBL through immunoinformatics identified several MHCI, MHCII and B cell epitopes throughout the peptide, with several of these lying in the M2 domain and being conserved between  P. vivax ,  P. yoelii  and  Plasmodium falciparum , hinting that the M2-MAEBL is pan-reactive. This hypothesis was tested through functional assays, showing that  P. yoelii  M2-MAEBL antisera are able to recognize and inhibit erythrocyte invasion from both  P. falciparum  and  P. vivax  parasites isolated from Thai patients, in ex vivo assays. Moreover, the sequence of the M2-MAEBL is shown to be highly conserved between  P. vivax  isolates from the Amazon and Thailand, indicating that the MAEBL antigen may constitute a vaccine candidate outwitting strain-specific immunity.    Conclusions  The MAEBL antigen is promising candidate towards the development of a malaria vaccine.    Electronic supplementary material  The online version of this article (10.1186/s12936-017-2144-x) contains supplementary material, which is available to authorized users.

In silico epitope mapping and experimental evaluation of the Merozoite Adhesive Erythrocytic Binding Protein (MAEBL) as a malaria vaccine candidate