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...

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Main Authors: Xiangye Liu, Huiqin Li, Hongkuan Deng, Chen Zheng, Hongru Yan, Zetian Chen, Anning Bian, Jiaxu Chen, Kuiyang Zheng
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-07-01
Series:Frontiers in Veterinary Science
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fvets.2019.00228/full
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author Xiangye Liu
Huiqin Li
Hongkuan Deng
Chen Zheng
Hongru Yan
Zetian Chen
Anning Bian
Jiaxu Chen
Kuiyang Zheng
author_facet Xiangye Liu
Huiqin Li
Hongkuan Deng
Chen Zheng
Hongru Yan
Zetian Chen
Anning Bian
Jiaxu Chen
Kuiyang Zheng
author_sort Xiangye Liu
collection DOAJ
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.
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spelling doaj.art-af74d4b5aa4f4abd94e08052766f99532022-12-21T17:32:54ZengFrontiers Media S.A.Frontiers in Veterinary Science2297-17692019-07-01610.3389/fvets.2019.00228471055Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding ProteinXiangye Liu0Huiqin Li1Hongkuan Deng2Chen Zheng3Hongru Yan4Zetian Chen5Anning Bian6Jiaxu Chen7Kuiyang Zheng8Jiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaSchool of Life Sciences, Shandong University of Technology, Zibo, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaKey Laboratory of Parasite and Vector Biology, Chinese Center for Disease Control and Prevention, WHO Collaborating Centre for Malaria, Schistosomiasis and Filariasis, Ministry of Health of China, National Institute of Parasitic Diseases, Shanghai, ChinaJiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, ChinaBabesia 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.https://www.frontiersin.org/article/10.3389/fvets.2019.00228/fullBabesia microtiglyceraldehyde-3-phosphate dehydrogenaseplasminogenα-actinbinding protein
spellingShingle Xiangye Liu
Huiqin Li
Hongkuan Deng
Chen Zheng
Hongru Yan
Zetian Chen
Anning Bian
Jiaxu Chen
Kuiyang Zheng
Glyceraldehyde-3-Phosphate Dehydrogenase of Babesia microti Is a Plasminogen- and Actin-Binding Protein
Frontiers in Veterinary Science
Babesia microti
glyceraldehyde-3-phosphate dehydrogenase
plasminogen
α-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 Babesia microti
glyceraldehyde-3-phosphate dehydrogenase
plasminogen
α-actin
binding protein
url https://www.frontiersin.org/article/10.3389/fvets.2019.00228/full
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