Structural Insights into the Cytotoxic Mechanism of Vibrio parahaemolyticus PirAvp and PirBvp Toxins

Lin, San‐Yih; Hsu, Kai Cheng; Wang, Hao Ching

doi:10.3390/md15120373

Cited by 49 publications

(65 citation statements)

References 58 publications

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“…Furthermore, PirA vp alone did not show activity against any type of erythrocytes tested. Possibly the A subunit participates in stabilizing the complex for a better binding to the possible receptor molecule on the shrimp hepatopancreatic epithelial cells [50]. These results highlight the importance of the interaction between the two subunits of the complex, which could act in molecular synergy to recognize the target molecule, as has been reported for the A and B subunits of the R. communis toxin [51].…”

Section: Discussionsupporting

confidence: 62%

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

et al. 2020

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Vibrio parahaemolyticus (Vp) is the etiological agent of the acute hepatopancreatic necrosis disease (AHPND) in Penaeus vannamei shrimp. Vp possesses a 63–70 kb conjugative plasmid that encodes the binary toxin PirAvp/PirBvp. The 250 kDa PirABvp complex was purified by affinity chromatography with galactose-sepharose 4B and on a stroma from glutaraldehyde-fixed rat erythrocytes column, as a heterotetramer of PirAvp and PirBvp subunits. In addition, recombinant pirB (rPirBvp) and pirA (rPirAvp) were obtained. The homogeneity of the purified protein was determined by SDS-PAGE analysis, and the yield of protein was 488 ng/100 μg of total protein of extracellular products. The PirABvp complex and the rPirBvp showed hemagglutinating activity toward rat erythrocytes. The rPirAvp showed no hemagglutinating capacity toward the animal red cells tested. Among different mono and disaccharides tested, only GalNH2 and GlcNH2 were able to inhibit hemagglutination of the PirABvp complex and the rPirBvp. Glycoproteins showed inhibitory specificity, and fetuin was the glycoprotein that showed the highest inhibition. Other glycoproteins, such as mucin, and glycosaminoglycans, such as heparin, also inhibited the activity. Desialylation of erythrocytes enhanced the hemagglutinating activity. This confirms that Gal or Gal (β1,4) GlcNAc are the main ligands for PirABvp. The agglutinating activity of the PirABvp complex and the rPirBvp is not dependent on cations, because addition of Mg2+ or Ca2+ showed no effect on the protein capacity. Our results strongly suggest that the PirBvp subunit is a lectin, which is part of the PirA/PirBvp complex, and it seems to participate in bacterial pathogenicity.

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Section: Discussionsupporting

confidence: 62%

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

et al. 2020

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“…To date, the cytotoxic mechanism of PirA/PirB is unclear, although the structures of PirA and PirB are very similar to those of insecticidal Cry toxins produced by Bacillus thuringiensis (Lin, Hsu, & Wang, ), which raises the possibility that their cytotoxic mechanisms are similar. Cry toxin contains three structural domains (domains I, II and III) connected by single linkers (Bravo, Gill, & Soberon, ).…”

Section: Discussionmentioning

confidence: 99%

“…If the role of PirA is similar to that of Cry toxin domain III, then PirA needs to interact with a sugar moiety of a receptor located on the host cell surface to facilitate the binding of domain II to another region in the receptor (Jenkins, Lee, Valaitis, Curtiss, & Dean, 2000). In fact, PirA has a possible sugar-binding pocket (Lin et al, 2017). Binding to this receptor then leads to the activation of domain I to form pores that will eventually cause cell lysis (Lin et al, 2017).…”

Section: Discussionmentioning

confidence: 99%

Anti‐PirA‐like toxin immunoglobulin (IgY) in feeds passively immunizes shrimp against acute hepatopancreatic necrosis disease

Nakamura

Pedrosa-Gerasmio

Alenton

et al. 2019

Journal of Fish Diseases

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Acute hepatopancreatic necrosis disease (AHPND), caused by a toxin‐producing Vibrio parahaemolyticus strain, has become a serious threat to shrimp aquaculture. The need to regulate antibiotic use prompted the development of alternative ways to treat infections in aquaculture including the use of chicken egg yolk immunoglobulin (IgY) for passive immunization. This study evaluated the protective effect of IgY against AHPND infection in Litopenaeus vannamei (Boone). IgY was isolated from eggs laid by hens immunized with recombinant PirA‐like (rPirA) and PirB‐like (rPirB) toxins. Whole‐egg powders having IgY specific to rPirA (anti‐PirA‐IgY) and rPirB (anti‐PirB‐IgY) and IgY from non‐immunized hen (control‐IgY) were mixed with basal diets at 20% concentrations and used to prefeed shrimp 3 days before the bacterial challenge test. Survival rates of the challenged shrimp fed the anti‐PirA‐IgY, anti‐PirB‐IgY and control‐IgY diets were 86%, 14% and 0%, respectively. Only the feed containing anti‐PirA‐IgY protected shrimp against AHPND. Increasing the concentration of rPirA antigen to immunize hens and lowering the amount of egg powder in feeds to 10% consistently showed higher survival rates in shrimp fed with anti‐PirA‐IgY (87%) compared with the control (12%). These results confirm that addition of anti‐PirA‐IgY in feeds could be an effective prophylactic method against AHPND infection in shrimp.

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“…Hepatopancreas histopathology shows inflammation and desquamation, while a hemocytic infiltrate is noted. This damage is produced by toxins PirAvp and PirBvp which have a structural similarity to B. thuringiensis Cry pore-forming toxin, so it has been suggested that PirAvp/PirBvp promote a similar process to induce cell death of the hepatopancreas tissue in shrimps [12,13]. Several strategies have been addressed to control diseases that affect a shrimp, such as tank water replacements, good personnel management practices, water monitoring, and use of antibiotics.…”

Section: Introductionmentioning

confidence: 99%

Silver Nanoparticles Synthesized with Rumex hymenosepalus: A Strategy to Combat Early Mortality Syndrome (EMS) in a Cultivated White Shrimp

Alvarez-Cirerol

López-Torres

Rodríguez-León

et al. 2019

Journal of Nanomaterials

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Early Mortality Syndrome (EMS) or Acute Hepatopancreatic Necrosis Syndrome (AHPNS) is a disease produced by gram-negative bacteria Vibrio parahaemolyticus (V. parahaemolyticus), which has caused declines in worldwide production of a white shrimp Litopenaeus vannamei (L. vannamei). In this work, we propose the implementation of silver nanoparticles (AgNPs) synthesized with Rumex hymenosepalus (Rh) extract as an alternative on V. parahaemolyticus control. AgNPs were characterized by UV-Vis spectroscopy, scanning electron microscopy (SEM), transmission electron microscopy (TEM), and selected area electron diffraction (SAED). AgNP mean sizes by DLS were 80.82±1.16 nm and sizes between 2 and 10 nm by TEM, with a zeta potential of −47.72±1.05 mV. This study evaluated AgNPs and Rh antimicrobial capacity on V. parahaemolyticus at different concentrations; the minimum inhibitory concentration (MIC) found was 25 μg/mL for AgNPs and 220 μg/mL for Rh. Additionally, were carried out time-kill curves and reactive oxygen species (ROS) generation for 1 and 4 MIC. Both concentrations (MIC) were tested for toxicity on Artemia nauplii from Artemia franciscana (A. franciscana), because nauplii were used as biocarriers for AgNPs and Rh extract on L. vannamei. Once the shrimp were treated, they were challenged with Vibrio infection and it was found that those who were treated with both agents showed greater survival than the control. V. parahaemolyticus and postlarval samples were taken from the bioassay and fixed and prepared for TEM and SEM in order to search NPs in internal structure of bacteria and the hepatopancreatic area of shrimps; AgNPs were detected in both cases. AgNPs and Rh extract show antibacterial properties on the infected shrimp with V. parahaemolyticus. The action mechanisms are interaction with the bacterial membrane and ROS generation; these effects are produced by both agents.

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Structural Insights into the Cytotoxic Mechanism of Vibrio parahaemolyticus PirAvp and PirBvp Toxins

Cited by 49 publications

References 58 publications

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

Anti‐PirA‐like toxin immunoglobulin (IgY) in feeds passively immunizes shrimp against acute hepatopancreatic necrosis disease

Silver Nanoparticles Synthesized with Rumex hymenosepalus: A Strategy to Combat Early Mortality Syndrome (EMS) in a Cultivated White Shrimp

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