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PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes
Upon invasion, Plasmodium falciparum exports hundreds of proteins across its surrounding parasitophorous vacuole membrane (PVM) to remodel the infected erythrocyte. Although this phenomenon is crucial for the parasite growth and virulence, elucidation of precise steps in the export pathway is still...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5829233/ https://www.ncbi.nlm.nih.gov/pubmed/29487358 http://dx.doi.org/10.1038/s41598-018-22026-0 |
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author | Morita, Masayuki Nagaoka, Hikaru Ntege, Edward H. Kanoi, Bernard N. Ito, Daisuke Nakata, Takahiro Lee, Ji-Won Tokunaga, Kazuaki Iimura, Tadahiro Torii, Motomi Tsuboi, Takafumi Takashima, Eizo |
author_facet | Morita, Masayuki Nagaoka, Hikaru Ntege, Edward H. Kanoi, Bernard N. Ito, Daisuke Nakata, Takahiro Lee, Ji-Won Tokunaga, Kazuaki Iimura, Tadahiro Torii, Motomi Tsuboi, Takafumi Takashima, Eizo |
author_sort | Morita, Masayuki |
collection | PubMed |
description | Upon invasion, Plasmodium falciparum exports hundreds of proteins across its surrounding parasitophorous vacuole membrane (PVM) to remodel the infected erythrocyte. Although this phenomenon is crucial for the parasite growth and virulence, elucidation of precise steps in the export pathway is still required. A translocon protein complex, PTEX, is the only known pathway that mediates passage of exported proteins across the PVM. P. falciparum Parasitophorous Vacuolar protein 1 (PfPV1), a previously reported parasitophorous vacuole (PV) protein, is considered essential for parasite growth. In this study, we characterized PfPV1 as a novel merozoite dense granule protein. Structured illumination microscopy (SIM) analyses demonstrated that PfPV1 partially co-localized with EXP2, suggesting the protein could be a PTEX accessory molecule. Furthermore, PfPV1 and exported protein PTP5 co-immunoprecipitated with anti-PfPV1 antibody. Surface plasmon resonance (SPR) confirmed the proteins’ direct interaction. Additionally, we identified a PfPV1 High-affinity Region (PHR) at the C-terminal side of PTP5 where PfPV1 dominantly bound. SIM analysis demonstrated an export arrest of PTP5ΔPHR, a PTP5 mutant lacking PHR, suggesting PHR is essential for PTP5 export to the infected erythrocyte cytosol. The overall results suggest that PfPV1, a novel dense granule protein, plays an important role in protein export at PV. |
format | Online Article Text |
id | pubmed-5829233 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58292332018-03-01 PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes Morita, Masayuki Nagaoka, Hikaru Ntege, Edward H. Kanoi, Bernard N. Ito, Daisuke Nakata, Takahiro Lee, Ji-Won Tokunaga, Kazuaki Iimura, Tadahiro Torii, Motomi Tsuboi, Takafumi Takashima, Eizo Sci Rep Article Upon invasion, Plasmodium falciparum exports hundreds of proteins across its surrounding parasitophorous vacuole membrane (PVM) to remodel the infected erythrocyte. Although this phenomenon is crucial for the parasite growth and virulence, elucidation of precise steps in the export pathway is still required. A translocon protein complex, PTEX, is the only known pathway that mediates passage of exported proteins across the PVM. P. falciparum Parasitophorous Vacuolar protein 1 (PfPV1), a previously reported parasitophorous vacuole (PV) protein, is considered essential for parasite growth. In this study, we characterized PfPV1 as a novel merozoite dense granule protein. Structured illumination microscopy (SIM) analyses demonstrated that PfPV1 partially co-localized with EXP2, suggesting the protein could be a PTEX accessory molecule. Furthermore, PfPV1 and exported protein PTP5 co-immunoprecipitated with anti-PfPV1 antibody. Surface plasmon resonance (SPR) confirmed the proteins’ direct interaction. Additionally, we identified a PfPV1 High-affinity Region (PHR) at the C-terminal side of PTP5 where PfPV1 dominantly bound. SIM analysis demonstrated an export arrest of PTP5ΔPHR, a PTP5 mutant lacking PHR, suggesting PHR is essential for PTP5 export to the infected erythrocyte cytosol. The overall results suggest that PfPV1, a novel dense granule protein, plays an important role in protein export at PV. Nature Publishing Group UK 2018-02-27 /pmc/articles/PMC5829233/ /pubmed/29487358 http://dx.doi.org/10.1038/s41598-018-22026-0 Text en © The Author(s) 2018 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 Morita, Masayuki Nagaoka, Hikaru Ntege, Edward H. Kanoi, Bernard N. Ito, Daisuke Nakata, Takahiro Lee, Ji-Won Tokunaga, Kazuaki Iimura, Tadahiro Torii, Motomi Tsuboi, Takafumi Takashima, Eizo PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title | PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title_full | PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title_fullStr | PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title_full_unstemmed | PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title_short | PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
title_sort | pv1, a novel plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5829233/ https://www.ncbi.nlm.nih.gov/pubmed/29487358 http://dx.doi.org/10.1038/s41598-018-22026-0 |
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