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

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 antibod...

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Autores principales: Zerka, Agata, Rydzak, Joanna, Lass, Anna, Szostakowska, Beata, Nahorski, Wacław, Wroczyńska, Agnieszka, Myjak, Przemyslaw, Krotkiewski, Hubert, Jaskiewicz, Ewa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4805696/
https://www.ncbi.nlm.nih.gov/pubmed/26439848
http://dx.doi.org/10.1007/s00005-015-0367-5
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author Zerka, Agata
Rydzak, Joanna
Lass, Anna
Szostakowska, Beata
Nahorski, Wacław
Wroczyńska, Agnieszka
Myjak, Przemyslaw
Krotkiewski, Hubert
Jaskiewicz, Ewa
author_facet Zerka, Agata
Rydzak, Joanna
Lass, Anna
Szostakowska, Beata
Nahorski, Wacław
Wroczyńska, Agnieszka
Myjak, Przemyslaw
Krotkiewski, Hubert
Jaskiewicz, Ewa
author_sort Zerka, Agata
collection PubMed
description 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.
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spelling pubmed-48056962016-04-09 Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand Zerka, Agata Rydzak, Joanna Lass, Anna Szostakowska, Beata Nahorski, Wacław Wroczyńska, Agnieszka Myjak, Przemyslaw Krotkiewski, Hubert Jaskiewicz, Ewa Arch Immunol Ther Exp (Warsz) Original Article 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. Springer International Publishing 2015-10-06 2016 /pmc/articles/PMC4805696/ /pubmed/26439848 http://dx.doi.org/10.1007/s00005-015-0367-5 Text en © The Author(s) 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Zerka, Agata
Rydzak, Joanna
Lass, Anna
Szostakowska, Beata
Nahorski, Wacław
Wroczyńska, Agnieszka
Myjak, Przemyslaw
Krotkiewski, Hubert
Jaskiewicz, Ewa
Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title_full Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title_fullStr Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title_full_unstemmed Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title_short Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand
title_sort studies on immunogenicity and antigenicity of baculovirus-expressed binding region of plasmodium falciparum eba-140 merozoite ligand
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4805696/
https://www.ncbi.nlm.nih.gov/pubmed/26439848
http://dx.doi.org/10.1007/s00005-015-0367-5
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