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Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment

The malarial parasite remodels the host erythrocyte following invasion. Well-known examples are adhesive proteins inserted into the host erythrocyte membrane, which function as virulence factors. The modification of the host erythrocyte may be mediated by a specialized domain of the endoplasmic reti...

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Autores principales: Cortés, Gladys T., Wiser, Mark F., Gómez-Alegría, Claudio J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7276435/
https://www.ncbi.nlm.nih.gov/pubmed/32529065
http://dx.doi.org/10.1016/j.heliyon.2020.e04037
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author Cortés, Gladys T.
Wiser, Mark F.
Gómez-Alegría, Claudio J.
author_facet Cortés, Gladys T.
Wiser, Mark F.
Gómez-Alegría, Claudio J.
author_sort Cortés, Gladys T.
collection PubMed
description The malarial parasite remodels the host erythrocyte following invasion. Well-known examples are adhesive proteins inserted into the host erythrocyte membrane, which function as virulence factors. The modification of the host erythrocyte may be mediated by a specialized domain of the endoplasmic reticulum, or Plasmodium export compartment (PEC). Previously, monoclonal antibodies recognizing the PEC were generated and one of these monoclonal antibodies recognize a 68 kDa parasite protein. In this study, the 68 kDa protein was affinity purified and analyzed by peptide mapping using mass spectrometry. The results demonstrate that the 68 kDa protein is the P. falciparum homolog of the endoplasmic reticulum resident HSP70 called PfHSP70-2. This finding is consistent with the PEC being a domain of the endoplasmic reticulum and suggests a role for PfHSP70-2 in the export of Plasmodium proteins into the host erythrocyte.
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spelling pubmed-72764352020-06-10 Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment Cortés, Gladys T. Wiser, Mark F. Gómez-Alegría, Claudio J. Heliyon Article The malarial parasite remodels the host erythrocyte following invasion. Well-known examples are adhesive proteins inserted into the host erythrocyte membrane, which function as virulence factors. The modification of the host erythrocyte may be mediated by a specialized domain of the endoplasmic reticulum, or Plasmodium export compartment (PEC). Previously, monoclonal antibodies recognizing the PEC were generated and one of these monoclonal antibodies recognize a 68 kDa parasite protein. In this study, the 68 kDa protein was affinity purified and analyzed by peptide mapping using mass spectrometry. The results demonstrate that the 68 kDa protein is the P. falciparum homolog of the endoplasmic reticulum resident HSP70 called PfHSP70-2. This finding is consistent with the PEC being a domain of the endoplasmic reticulum and suggests a role for PfHSP70-2 in the export of Plasmodium proteins into the host erythrocyte. Elsevier 2020-06-03 /pmc/articles/PMC7276435/ /pubmed/32529065 http://dx.doi.org/10.1016/j.heliyon.2020.e04037 Text en © 2020 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Cortés, Gladys T.
Wiser, Mark F.
Gómez-Alegría, Claudio J.
Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title_full Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title_fullStr Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title_full_unstemmed Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title_short Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment
title_sort identification of plasmodium falciparum hsp70-2 as a resident of the plasmodium export compartment
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7276435/
https://www.ncbi.nlm.nih.gov/pubmed/32529065
http://dx.doi.org/10.1016/j.heliyon.2020.e04037
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