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Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins

Plasmodium falciparum extensively remodels host cells by translocating numerous proteins into the cytoplasm of red blood cells (RBCs) after invasion. Among these exported proteins, members of the Plasmodium helical interspersed subtelomeric (PHIST) family are crucial for host cell remodeling and hos...

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Autores principales: Yang, Baoling, Wang, Xiaofeng, Jiang, Ning, Sang, Xiaoyu, Feng, Ying, Chen, Ran, Wang, Xinyi, Chen, Qijun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7691434/
https://www.ncbi.nlm.nih.gov/pubmed/33281807
http://dx.doi.org/10.3389/fmicb.2020.611190
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author Yang, Baoling
Wang, Xiaofeng
Jiang, Ning
Sang, Xiaoyu
Feng, Ying
Chen, Ran
Wang, Xinyi
Chen, Qijun
author_facet Yang, Baoling
Wang, Xiaofeng
Jiang, Ning
Sang, Xiaoyu
Feng, Ying
Chen, Ran
Wang, Xinyi
Chen, Qijun
author_sort Yang, Baoling
collection PubMed
description Plasmodium falciparum extensively remodels host cells by translocating numerous proteins into the cytoplasm of red blood cells (RBCs) after invasion. Among these exported proteins, members of the Plasmodium helical interspersed subtelomeric (PHIST) family are crucial for host cell remodeling and host-parasite interactions, and thereby contribute to malaria pathogenesis. Herein, we explored the function of PF3D7_1372300, a member of the PHIST/PHISTa-like subfamily. PF3D7_1372300 was highly transcribed and expressed during the blood stage of P. falciparum, and distributed throughout RBCs, but most abundant at the erythrocyte membrane. Specific interaction of PF3D7_1372300 with the cytoplasmic tail of P. falciparum erythrocyte membrane protein 1 (PfEMP1) was revealed by immunofluorescence assay, in vitro intermolecular interaction assays. The interaction sites of PF3D7_1372300 with PfEMP1 ATS domain were found involved more than 30 amino acids (aa) at several positions. The findings deepen our understanding of host-parasite interactions and malaria pathogenesis.
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spelling pubmed-76914342020-12-04 Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins Yang, Baoling Wang, Xiaofeng Jiang, Ning Sang, Xiaoyu Feng, Ying Chen, Ran Wang, Xinyi Chen, Qijun Front Microbiol Microbiology Plasmodium falciparum extensively remodels host cells by translocating numerous proteins into the cytoplasm of red blood cells (RBCs) after invasion. Among these exported proteins, members of the Plasmodium helical interspersed subtelomeric (PHIST) family are crucial for host cell remodeling and host-parasite interactions, and thereby contribute to malaria pathogenesis. Herein, we explored the function of PF3D7_1372300, a member of the PHIST/PHISTa-like subfamily. PF3D7_1372300 was highly transcribed and expressed during the blood stage of P. falciparum, and distributed throughout RBCs, but most abundant at the erythrocyte membrane. Specific interaction of PF3D7_1372300 with the cytoplasmic tail of P. falciparum erythrocyte membrane protein 1 (PfEMP1) was revealed by immunofluorescence assay, in vitro intermolecular interaction assays. The interaction sites of PF3D7_1372300 with PfEMP1 ATS domain were found involved more than 30 amino acids (aa) at several positions. The findings deepen our understanding of host-parasite interactions and malaria pathogenesis. Frontiers Media S.A. 2020-11-13 /pmc/articles/PMC7691434/ /pubmed/33281807 http://dx.doi.org/10.3389/fmicb.2020.611190 Text en Copyright © 2020 Yang, Wang, Jiang, Sang, Feng, Chen, Wang and Chen. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Yang, Baoling
Wang, Xiaofeng
Jiang, Ning
Sang, Xiaoyu
Feng, Ying
Chen, Ran
Wang, Xinyi
Chen, Qijun
Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title_full Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title_fullStr Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title_full_unstemmed Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title_short Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins
title_sort interaction analysis of a plasmodium falciparum phista-like protein and pfemp1 proteins
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7691434/
https://www.ncbi.nlm.nih.gov/pubmed/33281807
http://dx.doi.org/10.3389/fmicb.2020.611190
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