A novel Thioredoxin-related protein 14 from Fasciola gigantica has an immunodiagnostic potential for fasciolosis

Changklungmoa, Narin; Kueakhai, Pornanan; Sangpairoj, Kant; Osotprasit, Supawadee; Chaiwichien, Athit; Samrit, Tepparit; Sobhon, Prasert; Chaithirayanon, Kulathida

doi:10.1016/j.actatropica.2020.105471

Cited by 5 publications

(4 citation statements)

References 31 publications

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“…Protein-protein interactions are key to understanding the mechanisms of interaction between F. gigantica and the host [7,10,12,14,35,36]. We performed prediction analysis to identify the subcellular locations of the DEPs in the liver, hLNs, and spleen (Figure 4A and Table S5).…”

Section: Membrane and Extracellular Space Proteins Mediate Host Immune Responsementioning

confidence: 99%

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Proteomic Profiling of the Liver, Hepatic Lymph Nodes, and Spleen of Buffaloes Infected with Fasciola gigantica

Zhang

Elsheikha

et al. 2020

Pathogens

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In the present study, we used an isobaric tag for relative and absolute quantitation (iTRAQ) proteomics technology to characterize the differentially expressed proteins (DEPs) in the liver, hepatic lymph nodes (hLNs), and spleen of buffaloes infected with Fasciola gigantica (F. gigantica). We also used the parallel reaction monitoring (PRM) method to verify the expression levels of the DEPs in the three infected tissues. At three days post-infection (dpi), 225, 1821, and 364 DEPs were detected in the liver, hLNs, and spleen, respectively. At 42 dpi, 384, 252, and 214 DEPs were detected in the liver, hLNs, and spleen, respectively. At 70 dpi, 125, 829, and 247 DEPs were detected in the liver, hLNs, and spleen, respectively. Downregulation of metabolism was prominent in infected livers at all time points, and upregulation of immune responses was marked in the hLNs during early infection (three dpi); however, no changes in the immune response were detected at the late stages of infection (42 and 70 dpi). Compared to the hLNs, there was no significant upregulation in the levels of immune responses in the infected spleen. All the identified DEPs were used to predict the subcellular localization of the proteins, which were related to extracellular space and membrane and were involved in host immune responses. Further PRM analysis confirmed the expression of 18 proteins. These data provide the first simultaneous proteomic profiles of multiple organs of buffaloes experimentally infected with F. gigantica.

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Section: Membrane and Extracellular Space Proteins Mediate Host Immune Responsementioning

confidence: 99%

“…Control of fascioliasis in buffaloes is important because buffaloes are considered an economically vital livestock species in many developing countries [7,[11][12][13][14]. Due to the emergence of drug-resistance [15,16], there is a clear need for the development of vaccines and new flukicide drugs to effectively control fascioliasis.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Profiling of the Liver, Hepatic Lymph Nodes, and Spleen of Buffaloes Infected with Fasciola gigantica

Zhang

Elsheikha

et al. 2020

Pathogens

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“…Given that CL1 and GST showed good effects on the prevention and treatment of fascioliasis, the use of multistage-specific cocktails with better antigen-delivery systems and more small-molecule chemicals to elicit lethal or sub-lethal phenotypes would be considerable merit in vaccine development and drug target predictions in the future. Moreover, the phosphorylated effectors such as 14–3-3 and thioredoxin were also identified, and previous studies found that they could be recognized by sera from goats or mice experimentally infected with F. gigantica (Tian et al 2018 ; Changklungmoa et al 2020 ), making them considerable for immunodiagnostic candidates for fascioliasis.…”

Section: Discussionmentioning

confidence: 97%

A global phosphoproteomics analysis of adult Fasciola gigantica by LC–MS/MS

et al. 2022

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Protein phosphorylation plays key roles in a variety of essential cellular processes. Fasciola gigantica is a tropical liver fluke causing hepatobiliary disease fascioliasis, leading to human health threats and heavy economic losses. Although the genome and protein kinases of F. gigantica provided new insights to understand the molecular biology and etiology of this parasite, there is scant knowledge of protein phosphorylation events in F. gigantica . In this study, we characterized the global phosphoproteomics of adult F. gigantica by phosphopeptide enrichment-based LC–MS/MS, a high-throughput analysis to maximize the detection of a large repertoire of phosphoproteins and phosphosites. A total of 1030 phosphopeptides with 1244 phosphosites representing 635 F. gigantica phosphoproteins were identified. The phosphoproteins were involved in a wide variety of biological processes including cellular, metabolic, and single-organism processes. Meanwhile, these proteins were found predominantly in cellular components like membranes and organelles with molecular functions of binding (51.3%) and catalytic activity (40.6%). The KEGG annotation inferred that the most enriched pathways of the phosphoproteins included tight junction, spliceosome, and RNA transport (each one contains 15 identified proteins). Combining the reports in other protozoa and helminths, the phosphoproteins identified in this work play roles in metabolic regulation and signal transduction. To our knowledge, this work performed the first global phosphoproteomics analysis of adult F. gigantica , which provides valuable information for development of intervention strategies for fascioliasis. Supplementary Information The online version contains supplementary material available at 10.1007/s00436-021-07422-2.

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“…Wherefore, concentrating on phosphorylated enzymes recognized in this study, we can nd more effective targets and open new avenues to treat fascioliasis. In addition, phosphorylated effectors such us 14-3-3 and thioredoxin with good immuno-reactivity were also identi ed [34,35]. However, the phosphorylation processes catalyzed by gelsolin and calreticulin as well as tropomyosin had never been reported before, and BN1106_s378B000167 in particular deserved to mention as a result of hyper-phosphorylation (14 identi ed phosphopeptides) despite without any annotation, showing that BN1106_s378B000167 is unique in F. gigantica and can be used for subsequent functional studies and drug design in the future.…”

Section: Discussionmentioning

confidence: 99%

The Developmental Phosphoproteome of Fasciola Gigantica by Shotgun

Pan¹,

Bai²,

Gong³

et al. 2021

Preprint

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Background: Protein phosphorylation plays key roles in a variety of essential cellular processes. Fasciola gigantica is a tropical liver fluke causing hepatobiliary disease fascioliasis, leading to public health threats and heavy economic losses. Although the genome and protein kinases of F. gigantica provided novel insights to understand the molecular biology and etiology of this parasite, there is scant knowledge of protein phosphorylation events in F. gigantica. Results: In this study, we characterized the phosphoproteome of F. gigantica. A total of 1030 phosphopeptides and 1005 phosphorylation sites were identified in 635 F. gigantica phosphoproteins. The bioinformatic analyses and homologous comparisons of these phosphoproteins identified their features participating in cellular processes including metabolic regulation and signal transduction. Conclusions: To the best of our knowledge, this work performed the global phosphoproteomic analysis in F. gigantica, which provides a valuable resource to facilitate the development of novel interventions targets in F. gigantica and related nematodes in the future.

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A novel Thioredoxin-related protein 14 from Fasciola gigantica has an immunodiagnostic potential for fasciolosis

Cited by 5 publications

References 31 publications

Proteomic Profiling of the Liver, Hepatic Lymph Nodes, and Spleen of Buffaloes Infected with Fasciola gigantica

Proteomic Profiling of the Liver, Hepatic Lymph Nodes, and Spleen of Buffaloes Infected with Fasciola gigantica

A global phosphoproteomics analysis of adult Fasciola gigantica by LC–MS/MS

The Developmental Phosphoproteome of Fasciola Gigantica by Shotgun

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