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. 2016 Apr;64(2):149-56.
doi: 10.1007/s00005-015-0367-5. Epub 2015 Oct 6.

Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand

Agata Zerka  1 , Joanna Rydzak  1 , Anna Lass  2 , Beata Szostakowska  2 , Wacław Nahorski  3 , Agnieszka Wroczyńska  3 , Przemyslaw Myjak  2 , Hubert Krotkiewski  1 , Ewa Jaskiewicz  4   5
Affiliations

Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand

Agata Zerka et al. Arch Immunol Ther Exp (Warsz). 2016 Apr.

Erratum in

Abstract

The erythrocyte binding ligand 140 (EBA-140) is a member of the Plasmodium falciparum erythrocyte binding antigens (EBA) family, which are considered as prospective candidates for malaria vaccine development. EBA proteins were identified as important targets for naturally acquired inhibitory antibodies. Natural antibody response against EBA-140 ligand was found in individuals living in malaria-endemic areas. The EBA-140 ligand is a paralogue of the well-characterized P. falciparum EBA-175 protein. They both share homology of domain structure, including the binding region (Region II), which consists of two homologous F1 and F2 domains and is responsible for ligand-erythrocyte receptor interaction during merozoite invasion. It was shown that the erythrocyte receptor for EBA-140 ligand is glycophorin C-a minor human erythrocyte sialoglycoprotein. In studies on the immunogenicity of P. falciparum EBA ligands, the recombinant proteins are of great importance. In this report, we have demonstrated that the recombinant baculovirus-obtained EBA-140 Region II is immunogenic and antigenic. It can raise specific antibodies in rabbits, and it is recognized by natural antibodies present in sera of patients with malaria, and thus, it may be considered for inclusion in multicomponent blood-stage vaccines.

Keywords: Antigenicity; Immunogenicity; Natural anti-EBA-140 IgG antibodies; Plasmodium falciparum; Recombinant binding region of EBA-140 ligand; Region II baculovirus expression.

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Figures

Fig. 1
Fig. 1
Recognition of the recombinant EBA-140 Region II (RII) and its F2 domain fragment by MoAb (anti-myc, clone 9E10) and polyclonal rabbit antibodies (anti-RII) in Western blotting; bovine serum albumin (BSA), negative control
Fig. 2
Fig. 2
Binding of rabbit antibodies to the recombinant EBA-140 Region II and F2 domain fragment in ELISA (a). MoAb anti-myc (clone 9E10) was used as a positive binding control (b); BSA, negative control
Fig. 3
Fig. 3
a Binding of the recombinant EBA-140 Region II (RII) to human erythrocytes mesured in flow cytometry; b Inhibition of the erythrocyte binding of the recombinant EBA-140 Region II by rabbit antibodies (anti-RII)
Fig. 4
Fig. 4
Reactivity of human sera from persons with acute malaria (group 1, n = 25) and with the history of Plasmodium infection confirmed by serological examination (group 2, n = 11) with the recombinant EBA-140 Region II in ELISA
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