A bacterial binary toxin system that kills both insects and aquatic crustaceans: Photorhabdus insect-related toxins A and B

PLoS Pathog. 2023 May 4;19(5):e1011330. doi: 10.1371/journal.ppat.1011330. eCollection 2023 May.

Abstract

Photorhabdus insect-related toxins A and B (PirA and PirB) were first recognized as insecticidal toxins from Photorhabdus luminescens. However, subsequent studies showed that their homologs from Vibrio parahaemolyticus also play critical roles in the pathogenesis of acute hepatopancreatic necrosis disease (AHPND) in shrimps. Based on the structural features of the PirA/PirB toxins, it was suggested that they might function in the same way as a Bacillus thuringiensis Cry pore-forming toxin. However, unlike Cry toxins, studies on the PirA/PirB toxins are still scarce, and their cytotoxic mechanism remains to be clarified. In this review, based on our studies of V. parahaemolyticus PirAvp/PirBvp, we summarize the current understanding of the gene locations, expression control, activation, and cytotoxic mechanism of this type of toxin. Given the important role these toxins play in aquatic disease and their potential use in pest control applications, we also suggest further topics for research. We hope the information presented here will be helpful for future PirA/PirB studies.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Bacterial Toxins* / metabolism
  • Insecta / metabolism
  • Penaeidae* / microbiology
  • Photorhabdus* / metabolism
  • Vibrio parahaemolyticus* / metabolism

Substances

  • Bacterial Proteins
  • Bacterial Toxins

Grants and funding

This work was supported by Ministry of Science and Technology (grant number MOST 109-2313-B-038-001-MY3 to H.C.W, MOST 110-2313-B-006-001- to S.J.L); and the University System of Taipei Joint Research Program (USTP-NTOU-TMU-109-01 to H.C.W and J.H.L). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.