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Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes
Plasmodium falciparum causes the most severe form of malaria in humans and is responsible for over 700,000 deaths annually. It is an obligate intracellular parasite and invades erythrocytes where it grows in a relatively protected niche. Invasion of erythrocytes is essential for parasite survival an...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4356141/ https://www.ncbi.nlm.nih.gov/pubmed/25296023 http://dx.doi.org/10.7554/eLife.04187 |
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author | Chen, Lin Xu, Yibin Healer, Julie Thompson, Jenny K Smith, Brian J Lawrence, Michael C Cowman, Alan F |
author_facet | Chen, Lin Xu, Yibin Healer, Julie Thompson, Jenny K Smith, Brian J Lawrence, Michael C Cowman, Alan F |
author_sort | Chen, Lin |
collection | PubMed |
description | Plasmodium falciparum causes the most severe form of malaria in humans and is responsible for over 700,000 deaths annually. It is an obligate intracellular parasite and invades erythrocytes where it grows in a relatively protected niche. Invasion of erythrocytes is essential for parasite survival and this involves interplay of multiple protein–protein interactions. One of the most important interactions is binding of parasite invasion ligand families EBLs and PfRhs to host receptors on the surface of erythrocytes. PfRh5 is the only essential invasion ligand within the PfRh family and is an important vaccine candidate. PfRh5 binds the host receptor basigin. In this study, we have determined the crystal structure of PfRh5 using diffraction data to 2.18 Å resolution. PfRh5 exhibits a novel fold, comprising nine mostly anti-parallel α-helices encasing an N-terminal β-hairpin, with the overall shape being an elliptical disk. This is the first three-dimensional structure determined for the PfRh family of proteins. DOI: http://dx.doi.org/10.7554/eLife.04187.001 |
format | Online Article Text |
id | pubmed-4356141 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-43561412015-03-16 Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes Chen, Lin Xu, Yibin Healer, Julie Thompson, Jenny K Smith, Brian J Lawrence, Michael C Cowman, Alan F eLife Biophysics and Structural Biology Plasmodium falciparum causes the most severe form of malaria in humans and is responsible for over 700,000 deaths annually. It is an obligate intracellular parasite and invades erythrocytes where it grows in a relatively protected niche. Invasion of erythrocytes is essential for parasite survival and this involves interplay of multiple protein–protein interactions. One of the most important interactions is binding of parasite invasion ligand families EBLs and PfRhs to host receptors on the surface of erythrocytes. PfRh5 is the only essential invasion ligand within the PfRh family and is an important vaccine candidate. PfRh5 binds the host receptor basigin. In this study, we have determined the crystal structure of PfRh5 using diffraction data to 2.18 Å resolution. PfRh5 exhibits a novel fold, comprising nine mostly anti-parallel α-helices encasing an N-terminal β-hairpin, with the overall shape being an elliptical disk. This is the first three-dimensional structure determined for the PfRh family of proteins. DOI: http://dx.doi.org/10.7554/eLife.04187.001 eLife Sciences Publications, Ltd 2014-10-08 /pmc/articles/PMC4356141/ /pubmed/25296023 http://dx.doi.org/10.7554/eLife.04187 Text en © 2014, Chen et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biophysics and Structural Biology Chen, Lin Xu, Yibin Healer, Julie Thompson, Jenny K Smith, Brian J Lawrence, Michael C Cowman, Alan F Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title | Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title_full | Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title_fullStr | Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title_full_unstemmed | Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title_short | Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes |
title_sort | crystal structure of pfrh5, an essential p. falciparum ligand for invasion of human erythrocytes |
topic | Biophysics and Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4356141/ https://www.ncbi.nlm.nih.gov/pubmed/25296023 http://dx.doi.org/10.7554/eLife.04187 |
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