The opportunistic marine pathogen Vibrio parahaemolyticus becomes virulent by acquiring a plasmid that expresses a deadly toxin

Acute hepatopancreatic necrosis disease (AHPND) is a severe, newly emergent penaeid shrimp disease caused by Vibrio parahaemolyticus that has already led to tremendous losses in the cultured shrimp industry. Until now, its disease-causing mechanism has remained unclear. Here we show that an AHPND-ca...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2015-08, Vol.112 (34), p.10798-10803
Main Authors: Lee, Chung-Te, Chen, I-Tung, Yang, Yi-Ting, Ko, Tzu-Ping, Huang, Yun-Tzu, Huang, Jiun-Yan, Huang, Ming-Fen, Lin, Shin-Jen, Chen, Chien-Yu, Lin, Shih-Shun, Lin, Shih-Shuen, Lightner, Donald V, Wang, Han-Ching, Wang, Andrew H-J, Wang, Hao-Ching, Hor, Lien-I, Lo, Chu-Fang
Format: Article
Language:English
Subjects:
Animals
Bacillus
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Toxins - genetics
Bacterial Toxins - isolation & purification
Biological Sciences
Conjugation, Genetic
Crystal structure
Decapoda
DNA, Bacterial - genetics
Gangrene
Genes, Bacterial
Models, Molecular
Molecular Sequence Data
Open Reading Frames - genetics
Penaeidae - microbiology
Photorhabdus
Plasmids
Plasmids - genetics
Plasmids - metabolism
Porins - chemistry
Protein Conformation
Proteins
Sequence Homology, Nucleic Acid
Toxins
Vibrio parahaemolyticus
Vibrio parahaemolyticus - genetics
Vibrio parahaemolyticus - pathogenicity
Virulence - genetics
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Summary:Acute hepatopancreatic necrosis disease (AHPND) is a severe, newly emergent penaeid shrimp disease caused by Vibrio parahaemolyticus that has already led to tremendous losses in the cultured shrimp industry. Until now, its disease-causing mechanism has remained unclear. Here we show that an AHPND-causing strain of V. parahaemolyticus contains a 70-kbp plasmid (pVA1) with a postsegregational killing system, and that the ability to cause disease is abolished by the natural absence or experimental deletion of the plasmid-encoded homologs of the Photorhabdus insect-related (Pir) toxins PirA and PirB. We determined the crystal structure of the V. parahaemolyticus PirA and PirB (PirA(vp) and PirB(vp)) proteins and found that the overall structural topology of PirA(vp)/PirB(vp) is very similar to that of the Bacillus Cry insecticidal toxin-like proteins, despite the low sequence identity (
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1503129112