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Structural Insights to the Heterotetrameric Interaction between the Vibrio parahaemolyticus PirAvp and PirBvp Toxins and Activation of the Cry-Like Pore-Forming Domain

1
Department of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 701, Taiwan
2
The Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University and Academia Sinica, Taipei 110, Taiwan
3
Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110, Taiwan
4
Graduate Institute of Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei 110, Taiwan
5
Ph.D. Program for Cancer Molecular Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei 110, Taiwan
6
Biomedical Commercialization Center, Taipei Medical University, Taipei 110, Taiwan
7
Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan
8
International Center for the Scientific Development of Shrimp Aquaculture, National Cheng Kung University, Tainan 701, Taiwan
*
Author to whom correspondence should be addressed.
Toxins 2019, 11(4), 233; https://doi.org/10.3390/toxins11040233
Received: 26 March 2019 / Revised: 16 April 2019 / Accepted: 19 April 2019 / Published: 22 April 2019
(This article belongs to the Special Issue Pore-Forming Toxins (PFTs): Never Out of Fashion)
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Abstract

Acute hepatopancreatic necrosis disease (AHPND) is a newly emergent penaeid shrimp disease which can cause 70–100% mortality in Penaeus vannamei and Penaeus monodon, and has resulted in enormous economic losses since its appearance. AHPND is caused by the specific strains of Vibrio parahaemolyticus that harbor the pVA1 plasmid and express PirAvp and PirBvp toxins. These two toxins have been reported to form a binary complex. When both are present, they lead to the death of shrimp epithelial cells in the hepatopancreas and cause the typical histological symptoms of AHPND. However, the binding mode of PirAvp and PirBvp has not yet been determined. Here, we used isothermal titration calorimetry (ITC) to measure the binding affinity of PirAvp and PirBvp. Since the dissociation constant (Kd = 7.33 ± 1.20 μM) was considered too low to form a sufficiently stable complex for X-ray crystallographic analysis, we used alternative methods to investigate PirAvp-PirBvp interaction, first by using gel filtration to evaluate the molecular weight of the PirAvp/PirBvp complex, and then by using cross-linking and hydrogen-deuterium exchange (HDX) mass spectrometry to further understand the interaction interface between PirAvp and PirBvp. Based on these results, we propose a heterotetrameric interaction model of this binary toxin complex. This model provides insight of how conformational changes might activate the PirBvp N-terminal pore-forming domain and should be helpful for devising effective anti-AHPND strategies in the future. View Full-Text
Keywords: Vibrio parahaemolyticus; AHPND; PirAvp; PirBvp; protein-protein interaction Vibrio parahaemolyticus; AHPND; PirAvp; PirBvp; protein-protein interaction
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Lin, S.-J.; Chen, Y.-F.; Hsu, K.-C.; Chen, Y.-L.; Ko, T.-P.; Lo, C.-F.; Wang, H.-C.; Wang, H.-C. Structural Insights to the Heterotetrameric Interaction between the Vibrio parahaemolyticus PirAvp and PirBvp Toxins and Activation of the Cry-Like Pore-Forming Domain. Toxins 2019, 11, 233.

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