Research output per year
Research output per year
Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.7
Classification:TOXIN
Release Date:2015-08-26
Deposition Date:2014-10-22
Revision Date:2017-11-22
Molecular Weight:102515.7
Macromolecule Type:Protein
Residue Count:892
Atom Site Count:6854
DOI:10.2210/pdb3x0u/pdb
Abstract:
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 (
Resolution:1.7
Classification:TOXIN
Release Date:2015-08-26
Deposition Date:2014-10-22
Revision Date:2017-11-22
Molecular Weight:102515.7
Macromolecule Type:Protein
Residue Count:892
Atom Site Count:6854
DOI:10.2210/pdb3x0u/pdb
Abstract:
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 (
| Date made available | 2015 |
|---|---|
| Publisher | RCSB-PDB |
Research output
- 1 Article
-
The opportunistic marine pathogen Vibrio parahaemolyticus becomes virulent by acquiring a plasmid that expresses a deadly toxin
Lee, C. T., Chen, I. T., Yang, Y. T., Ko, T. P., Huang, Y. T., Huang, J. Y., Huang, M. F., Lin, S. J., Chen, C. Y., Lin, S. S., Lightner, D. V., Wang, H. C., Wang, A. H. J., Wang, H. C., Hor, L. I. & Lo, C. F., Aug 25 2015, In: Proceedings of the National Academy of Sciences of the United States of America. 112, 34, p. 10798-10803 6 p.Research output: Contribution to journal › Article › peer-review
Open Access439 Citations (Scopus)