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Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion

Malaria remains a major health problem worldwide. All clinical symptoms of malaria are attributed to the asexual blood stages of the parasite life cycle. Proteins resident in apical organelles and present on the surface of P. falciparum merozoites are considered promising candidates for the developm...

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Autores principales: Hans, Nidhi, Singh, Shailja, Pandey, Alok K., Reddy, K. Sony, Gaur, Deepak, Chauhan, Virander S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772933/
https://www.ncbi.nlm.nih.gov/pubmed/24058628
http://dx.doi.org/10.1371/journal.pone.0074790
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author Hans, Nidhi
Singh, Shailja
Pandey, Alok K.
Reddy, K. Sony
Gaur, Deepak
Chauhan, Virander S.
author_facet Hans, Nidhi
Singh, Shailja
Pandey, Alok K.
Reddy, K. Sony
Gaur, Deepak
Chauhan, Virander S.
author_sort Hans, Nidhi
collection PubMed
description Malaria remains a major health problem worldwide. All clinical symptoms of malaria are attributed to the asexual blood stages of the parasite life cycle. Proteins resident in apical organelles and present on the surface of P. falciparum merozoites are considered promising candidates for the development of blood stage malaria vaccines. In the present study, we have identified and characterized a microneme associated antigen, PfMA [PlasmoDB Gene ID: PF3D7_0316000, PFC0700c]. The gene was selected by applying a set of screening criteria such as transcriptional upregulation at late schizogony, inter-species conservation and the presence of signal sequence or transmembrane domains. The gene sequence of PfMA was found to be conserved amongst various Plasmodium species. We experimentally demonstrated that the transcript for PfMA was expressed only in the late blood stages of parasite consistent with a putative role in erythrocyte invasion. PfMA was localized by immunofluorescence and immuno-electron microscopy to be in the micronemes, an apical organelle of merozoites. The functional role of the PfMA protein in erythrocyte invasion was identified as a parasite adhesin involved in direct attachment with the target erythrocyte. PfMA was demonstrated to bind erythrocytes in a sialic acid independent, chymotrypsin and trypsin resistant manner and its antibodies inhibited P. falciparum erythrocyte invasion. Invasion of erythrocytes is a complex multistep process that involves a number of redundant ligand-receptor interactions many of which still remain unknown and even uncharacterized. Our work has identified and characterized a novel P. falciparum adhesin involved in erythrocyte invasion.
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spelling pubmed-37729332013-09-20 Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion Hans, Nidhi Singh, Shailja Pandey, Alok K. Reddy, K. Sony Gaur, Deepak Chauhan, Virander S. PLoS One Research Article Malaria remains a major health problem worldwide. All clinical symptoms of malaria are attributed to the asexual blood stages of the parasite life cycle. Proteins resident in apical organelles and present on the surface of P. falciparum merozoites are considered promising candidates for the development of blood stage malaria vaccines. In the present study, we have identified and characterized a microneme associated antigen, PfMA [PlasmoDB Gene ID: PF3D7_0316000, PFC0700c]. The gene was selected by applying a set of screening criteria such as transcriptional upregulation at late schizogony, inter-species conservation and the presence of signal sequence or transmembrane domains. The gene sequence of PfMA was found to be conserved amongst various Plasmodium species. We experimentally demonstrated that the transcript for PfMA was expressed only in the late blood stages of parasite consistent with a putative role in erythrocyte invasion. PfMA was localized by immunofluorescence and immuno-electron microscopy to be in the micronemes, an apical organelle of merozoites. The functional role of the PfMA protein in erythrocyte invasion was identified as a parasite adhesin involved in direct attachment with the target erythrocyte. PfMA was demonstrated to bind erythrocytes in a sialic acid independent, chymotrypsin and trypsin resistant manner and its antibodies inhibited P. falciparum erythrocyte invasion. Invasion of erythrocytes is a complex multistep process that involves a number of redundant ligand-receptor interactions many of which still remain unknown and even uncharacterized. Our work has identified and characterized a novel P. falciparum adhesin involved in erythrocyte invasion. Public Library of Science 2013-09-13 /pmc/articles/PMC3772933/ /pubmed/24058628 http://dx.doi.org/10.1371/journal.pone.0074790 Text en © 2013 Hans et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Hans, Nidhi
Singh, Shailja
Pandey, Alok K.
Reddy, K. Sony
Gaur, Deepak
Chauhan, Virander S.
Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title_full Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title_fullStr Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title_full_unstemmed Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title_short Identification and Characterization of a Novel Plasmodium falciparum Adhesin Involved in Erythrocyte Invasion
title_sort identification and characterization of a novel plasmodium falciparum adhesin involved in erythrocyte invasion
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772933/
https://www.ncbi.nlm.nih.gov/pubmed/24058628
http://dx.doi.org/10.1371/journal.pone.0074790
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