A Review of the Functional Annotations of Important Genes in the AHPND-Causing pVA1 Plasmid

Wang, Hao Ching; Lin, San‐Yih; Mohapatra, Arpita; Kumar, Ramya; Wang, Han Ching

doi:10.3390/microorganisms8070996

Cited by 17 publications

(22 citation statements)

References 79 publications

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“…Most studies have revealed that the AHPND causing bacteria usually release their toxins after invading the digestive tract, which results in the production of the characteristic symptoms [ 14 , 17 , 40 ]. Although the details of the molecular mechanisms involved in the pathogenesis of AHPND are still unknown, it is believed that PirA and PirB form a heterodimer that binds to receptors, after which PirB enters the cell through pore formation and then circulates to the hepatopancreas where it exerts cellular damage including sloughing of epithelial cells into the lumen (see recent reviews by [ 41 , 42 ]). Thus, damage to the hepatopancreatic tubules allows PirB toxin to be released into the intertubular space, which is then carried into hemolymph to infect hemocytes.…”

Section: Discussionmentioning

confidence: 99%

The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei

Zheng

Aweya

et al. 2021

Virulence

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Acute hepatopancreatic necrosis disease (AHPND) is a major debilitating disease that causes massive shrimp death resulting in substantial economic losses in shrimp aquaculture. The Pir toxin proteins secreted by a unique strain of Vibrio parahaemolyticus play an essential role in the pathogenesis of AHPND. At present, most studies on the effects of Pir toxin proteins in shrimp focus on digestive tissues or organs such as hepatopancreas, stomach, etc., with none on the immune organs. In the present study, two recombinant Pir toxin proteins (rPirA and rPirB) of V. parahaemolyticus were expressed with rPirB shown to enter shrimp hemocytes. Employing pull-down and LC-MS/MS analysis, GST-rPirB was found to interact with 13 proteins in hemocytes, including histone H3 and histone H4 and among which histone H4 had the highest protein score. Further analysis using GST pull-down and Far-Western blot analysis revealed that rPirB could interact with histone H4. In addition, using the purified nucleosome protein from Drosophila S2 cells, it was found that PirB protein could specifically bind to histones. When flow cytometry was applied, it was observed that the interaction between PirB and histones in shrimp hemocytes induces apoptosis, which results in the dephosphorylation of Serine 10 in histone H3. Collectively, the current study shows that in addition to its effect on the digestive tract of shrimp, the PirB toxin protein interacts with histones to affect the phosphorylation of histone H3-S10, thereby inducing apoptosis.

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Section: Discussionmentioning

confidence: 99%

The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei

Zheng

Aweya

et al. 2021

Virulence

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“…Transposases are enzymes that are involved in the translocation of DNA transposons to another location in the plasmid and/or genome (Harmer et al 2020). In fact, more than one transposase gene can be found in a single plasmid, likely due to the heteromeric structure of some of these enzymes (Peters et al 2014;Wang et al 2020).…”

Section: R a F Tmentioning

confidence: 99%

Identification of plasmids from Brazilian Chromobacterium violaceum strains

et al. 2022

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Chromobacterium violaceum is an opportunistic pathogen found in tropical and subtropical regions worldwide. Chromobacterium violaceum infections are difficult to treat, and many strains are resistant to antibiotics. Recently, a novel plasmid (pChV1) was discovered in the type strain ATCC 12472, suggesting that other C. violaceum strains may harbor extra-chromosomal DNA. The aim of the present study was to detect and compare new plasmids in Brazilian strains of C. violaceum using next-generation sequencing techniques. We obtained draft genomes of six plasmids from strains isolated from the Amazon region and aligned them with pChV1. At least three plasmids, CVAC05, CVACO2, and CVT8, were similar to pChV1. Phylogenetic analysis suggested that these new extra-chromosomal DNA sequences have a common origin with pChV1 but have diverged. Many of the ORFs detected were related to plasmid segregation/maintenance, viral structural proteins, and proteins with unknown functions. These findings may enable better genetic manipulation of C. violaceum, which will enhance our ability to exploit this valuable microorganism in industrial and clinical applications.

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“…The PirA vp and PirB vp genes are part of the same operon ( 18 ). The genes are synchronously regulated and expressed ( 19 ). However, how VP AHPND colonizes the stomach, hepatopancreas, and intestinal tract, and how the PirA vp and PirB vp toxins interact with these tissues are unknown.…”

Section: Introductionmentioning

confidence: 99%

“…Structural analyses have revealed the functional relationship between PirA vp /PirB vp and the Cry toxin of Bacillus thuringiensis ( 19 ). The Cry pore-forming toxin includes three functional domains: N-terminal pore-forming domain I, middle receptor binding domain II, and C-terminal sugar/receptor binding domain III ( 19 ). The toxic mechanism of Cry toxins involves the recognition of n-acetylgalactosamine, which is present on several receptors, by domain III.…”

Section: Introductionmentioning

confidence: 99%

Identification and Expression Analysis of an Interacting Protein (LvFABP) that Mediates Vibrio parahaemolyticus AHPND Toxin Action

Liu

Wang

et al. 2022

Front. Immunol.

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Acute hepatopancreatic necrosis disease (AHPND) caused by Vibrio parahaemolyticus causing AHPND (VPAHPND) is the most serious disease affecting shrimp farming. The PirAvp and PirBvp toxins of VPAHPND are known virulence factors. However, the corresponding target protein in shrimp that mediates their action has not been identified. By screening yeast two-hybrid cDNA libraries from intestine, stomach, and hepatopancreas of Litopenaeus vannamei, the protein with the largest increase in gene expression in shrimp hepatopancreas in response to VPAHPND challenge was identified and designated LvFABP. Analysis revealed high sequence homology of the LvFABP gene and a lipocalin/cytosolic fatty acid binding gene. Yeast two-hybrid pairwise analysis, GST-pull down assay, and far-western blot assay were performed to determine the interaction between LvFABP and PirBvp. LvFABP was able to directly bind to PirBvp. The expression of LvFABP in the hepatopancreas was significantly higher at P23 and P27 developmental stages of L. vannamei. RNA interference (RNAi) of LvFABP reduced the mortality, histopathological signs of AHPND in the hepatopancreas, and the number of virulent VPAHPND bacteria in the intestine, stomach, and hepatopancreas after VPAHPND challenge. We concluded that the LvFABP was involved in AHPND pathogenesis and acted as a VPAHPND toxin interacting protein. This is the first identification of VPAHPND toxin interacting protein from the shrimp digestive system by yeast two-hybrid library screening and were confirmed by in vitro protein interaction verification and in vivo challenge experiments. This study provides novel insight into the contributions of LvFABP towards AHPND pathogenesis in shrimp. The findings could inform AHPND preventative measures in shrimp farming.

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A Review of the Functional Annotations of Important Genes in the AHPND-Causing pVA1 Plasmid

Cited by 17 publications

References 79 publications

The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei

The PirB toxin protein from Vibrio parahaemolyticus induces apoptosis in hemocytes of Penaeus vannamei

Identification of plasmids from Brazilian Chromobacterium violaceum strains

Identification and Expression Analysis of an Interacting Protein (LvFABP) that Mediates Vibrio parahaemolyticus AHPND Toxin Action

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