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PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47)
Malaria symptoms and pathology are initiated by invasion of host erythrocytes by Plasmodium merozoites in a complex process that involves interactions between parasite and host erythrocyte proteins. Erythrocyte invasion presents attractive targets for malaria vaccine and drug development. Recently i...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6459815/ https://www.ncbi.nlm.nih.gov/pubmed/30976034 http://dx.doi.org/10.1038/s41598-019-42366-9 |
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author | Nagaoka, Hikaru Sasaoka, Chisa Yuguchi, Takaaki Kanoi, Bernard N. Ito, Daisuke Morita, Masayuki Udomsangpetch, Rachanee Sattabongkot, Jetsumon Ishino, Tomoko Tsuboi, Takafumi Takashima, Eizo |
author_facet | Nagaoka, Hikaru Sasaoka, Chisa Yuguchi, Takaaki Kanoi, Bernard N. Ito, Daisuke Morita, Masayuki Udomsangpetch, Rachanee Sattabongkot, Jetsumon Ishino, Tomoko Tsuboi, Takafumi Takashima, Eizo |
author_sort | Nagaoka, Hikaru |
collection | PubMed |
description | Malaria symptoms and pathology are initiated by invasion of host erythrocytes by Plasmodium merozoites in a complex process that involves interactions between parasite and host erythrocyte proteins. Erythrocyte invasion presents attractive targets for malaria vaccine and drug development. Recently it was observed that antibodies against PfMSA180 (PF3D7_1014100) are associated with protection from symptomatic malaria, suggesting that this protein is a target of naturally acquired protective antibodies. Here we characterize PfMSA180, a ~170 kDa merozoite surface antigen that is potentially involved in erythrocyte invasion. PfMSA180 synthesized by the wheat germ cell-free system was used to raise antibodies in rabbits. Growth inhibition assays revealed that parasite invasion is inhibited by antibodies to the PfMSA180 C-terminal region, which contains an erythrocyte-binding domain. Surface plasmon resonance analysis showed that PfMSA180 specifically interacts with human erythrocyte integrin associated protein (CD47), suggesting that PfMSA180 plays a role during merozoite invasion of erythrocytes. Polymorphism analysis revealed that pfmsa180 is highly conserved among field isolates. We show that naturally acquired PfMSA180-specific antibodies responses are associated with protective immunity in a malaria-exposed Thai population. In sum, the data presented here supports further evaluation of the conserved erythrocyte-binding C-terminal region of PfMSA180 as an asexual blood-stage malaria vaccine candidate. |
format | Online Article Text |
id | pubmed-6459815 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64598152019-04-16 PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) Nagaoka, Hikaru Sasaoka, Chisa Yuguchi, Takaaki Kanoi, Bernard N. Ito, Daisuke Morita, Masayuki Udomsangpetch, Rachanee Sattabongkot, Jetsumon Ishino, Tomoko Tsuboi, Takafumi Takashima, Eizo Sci Rep Article Malaria symptoms and pathology are initiated by invasion of host erythrocytes by Plasmodium merozoites in a complex process that involves interactions between parasite and host erythrocyte proteins. Erythrocyte invasion presents attractive targets for malaria vaccine and drug development. Recently it was observed that antibodies against PfMSA180 (PF3D7_1014100) are associated with protection from symptomatic malaria, suggesting that this protein is a target of naturally acquired protective antibodies. Here we characterize PfMSA180, a ~170 kDa merozoite surface antigen that is potentially involved in erythrocyte invasion. PfMSA180 synthesized by the wheat germ cell-free system was used to raise antibodies in rabbits. Growth inhibition assays revealed that parasite invasion is inhibited by antibodies to the PfMSA180 C-terminal region, which contains an erythrocyte-binding domain. Surface plasmon resonance analysis showed that PfMSA180 specifically interacts with human erythrocyte integrin associated protein (CD47), suggesting that PfMSA180 plays a role during merozoite invasion of erythrocytes. Polymorphism analysis revealed that pfmsa180 is highly conserved among field isolates. We show that naturally acquired PfMSA180-specific antibodies responses are associated with protective immunity in a malaria-exposed Thai population. In sum, the data presented here supports further evaluation of the conserved erythrocyte-binding C-terminal region of PfMSA180 as an asexual blood-stage malaria vaccine candidate. Nature Publishing Group UK 2019-04-11 /pmc/articles/PMC6459815/ /pubmed/30976034 http://dx.doi.org/10.1038/s41598-019-42366-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Nagaoka, Hikaru Sasaoka, Chisa Yuguchi, Takaaki Kanoi, Bernard N. Ito, Daisuke Morita, Masayuki Udomsangpetch, Rachanee Sattabongkot, Jetsumon Ishino, Tomoko Tsuboi, Takafumi Takashima, Eizo PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title | PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title_full | PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title_fullStr | PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title_full_unstemmed | PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title_short | PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47) |
title_sort | pfmsa180 is a novel plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (cd47) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6459815/ https://www.ncbi.nlm.nih.gov/pubmed/30976034 http://dx.doi.org/10.1038/s41598-019-42366-9 |
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