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Identification, characterization and heparin binding capacity of a spore-wall, virulence protein from the shrimp microsporidian, Enterocytozoon hepatopenaei (EHP)
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Metadata
Document Title
Identification, characterization and heparin binding capacity of a spore-wall, virulence protein from the shrimp microsporidian, Enterocytozoon hepatopenaei (EHP)
Author
Jaroenlak P., Boakye D.W., Vanichviriyakit R., Williams B.A.P., Sritunyalucksana K., Itsathitphaisarn O.
Name from Authors Collection
Affiliations
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand; Center of Excellence for Shrimp Molecular Biology and Biotechnology (Centex Shrimp), Faculty of Science, Mahidol University, Bangkok, Thailand; Biosciences, College of Life and Environmental Sciences, University of Exeter, Devon, United Kingdom; Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand; National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), Pathumthani, Thailand; Shrimp Pathogen Interaction Laboratory (SPI), National Center for Genetic Engineering and Biotechnology (BIOTEC), Bangkok, Thailand
Type
Article
Source Title
Parasites and Vectors
ISSN
17563305
Year
2018
Volume
11
Issue
1
Open Access
Gold, Green
Publisher
BioMed Central Ltd.
DOI
10.1186/s13071-018-2758-z
Abstract
Background: The microsporidian Enterocytozoon hepatopenaei (EHP) is a spore-forming, intracellular parasite that causes an economically debilitating disease (hepatopancreatic microsporidiosis or HPM) in cultured shrimp. HPM is characterized by growth retardation and wide size variation that can result in economic loss for shrimp farmers. Currently, the infection mechanism of EHP in shrimp is poorly understood, especially at the level of host-parasite interaction. In other microsporidia, spore wall proteins have been reported to be involved in host cell recognition. For the host, heparin, a glycosaminoglycan (GAG) molecule found on cell surfaces, has been shown to be recognized by many parasites such as Plasmodium spp. and Leishmania spp. Results: We identified and characterized the first spore wall protein of EHP (EhSWP1). EhSWP1 contains three heparin binding motifs (HBMs) at its N-terminus and a Bin-amphiphysin-Rvs-2 (BAR2) domain at its C-terminus. A phylogenetic analysis revealed that EhSWP1 is similar to an uncharacterized spore wall protein from Enterospora canceri. In a cohabitation bioassay using EHP-infected shrimp with naïve shrimp, the expression of EhSWP1 was detected by RT-PCR in the naïve test shrimp at 20 days after the start of cohabitation. Immunofluorescence analysis confirmed that EhSWP1 was localized in the walls of purified, mature spores. Subcellular localization by an immunoelectron assay revealed that EhSWP1 was distributed in both the endospore and exospore layers. An in vitro binding assay, a competition assay and mutagenesis studies revealed that EhSWP1 is a bona fide heparin binding protein. Conclusions: Based on our results, we hypothesize that EhSWP1 is an important host-parasite interaction protein involved in tethering spores to host-cell-surface heparin during the process of infection. © 2018 The Author(s).
Keyword
EHP | Enterocytozoon hepatopenaei | Heparin | Heparin binding protein | Spore wall protein | SWP
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
Funding Sponsor
Mahidol University; Thailand Research Fund; Agricultural Research Development Agency; School of Aerospace Science and Technology
License
CC BY
Rights
Author
Publication Source
Scopus