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Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein
Babesia microti, an intraerythrocytic protozoa, can cause an emerging tick-borne disease—Human babesiosis. The parasite can successfully invade host red blood cells owing to the assistance of molecules expressed by babesia. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the housekeeping intracell...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637311/ https://www.ncbi.nlm.nih.gov/pubmed/31355216 http://dx.doi.org/10.3389/fvets.2019.00228 |
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author | Liu, Xiangye Li, Huiqin Deng, Hongkuan Zheng, Chen Yan, Hongru Chen, Zetian Bian, Anning Chen, Jiaxu Zheng, Kuiyang |
author_facet | Liu, Xiangye Li, Huiqin Deng, Hongkuan Zheng, Chen Yan, Hongru Chen, Zetian Bian, Anning Chen, Jiaxu Zheng, Kuiyang |
author_sort | Liu, Xiangye |
collection | PubMed |
description | Babesia microti, an intraerythrocytic protozoa, can cause an emerging tick-borne disease—Human babesiosis. The parasite can successfully invade host red blood cells owing to the assistance of molecules expressed by babesia. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the housekeeping intracellular glycolytic enzyme, can also be expressed in the external of cells, where contributes to binding to several molecules such as plasminogen and actin. In the present study, we identified B. microti GAPDH (BmGAPDH) and generated the recombinant BmGAPDH (rBmGAPDH) via an E. coli expression system. Furthermore, we confirmed its catalytic dehydration activity in vitro. Moreover, we also demonstrated that rBmGAPDH could bind to human plasminogen and mouse α-actin. In addition, we demonstrated that rBmGAPDH could recognize anti-B. microti mouse serum. In conclusion, BmGAPDH is a multifunctional glycolytic enzyme, which can bind to host plasminogen and α-actin. |
format | Online Article Text |
id | pubmed-6637311 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-66373112019-07-26 Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein Liu, Xiangye Li, Huiqin Deng, Hongkuan Zheng, Chen Yan, Hongru Chen, Zetian Bian, Anning Chen, Jiaxu Zheng, Kuiyang Front Vet Sci Veterinary Science Babesia microti, an intraerythrocytic protozoa, can cause an emerging tick-borne disease—Human babesiosis. The parasite can successfully invade host red blood cells owing to the assistance of molecules expressed by babesia. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the housekeeping intracellular glycolytic enzyme, can also be expressed in the external of cells, where contributes to binding to several molecules such as plasminogen and actin. In the present study, we identified B. microti GAPDH (BmGAPDH) and generated the recombinant BmGAPDH (rBmGAPDH) via an E. coli expression system. Furthermore, we confirmed its catalytic dehydration activity in vitro. Moreover, we also demonstrated that rBmGAPDH could bind to human plasminogen and mouse α-actin. In addition, we demonstrated that rBmGAPDH could recognize anti-B. microti mouse serum. In conclusion, BmGAPDH is a multifunctional glycolytic enzyme, which can bind to host plasminogen and α-actin. Frontiers Media S.A. 2019-07-09 /pmc/articles/PMC6637311/ /pubmed/31355216 http://dx.doi.org/10.3389/fvets.2019.00228 Text en Copyright © 2019 Liu, Li, Deng, Zheng, Yan, Chen, Bian, Chen and Zheng. 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 | Veterinary Science Liu, Xiangye Li, Huiqin Deng, Hongkuan Zheng, Chen Yan, Hongru Chen, Zetian Bian, Anning Chen, Jiaxu Zheng, Kuiyang Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title | Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title_full | Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title_fullStr | Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title_full_unstemmed | Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title_short | Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein |
title_sort | glyceraldehyde-3-phosphate dehydrogenase of babesia microti is a plasminogen- and actin-binding protein |
topic | Veterinary Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637311/ https://www.ncbi.nlm.nih.gov/pubmed/31355216 http://dx.doi.org/10.3389/fvets.2019.00228 |
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