Differential proteomics analysis of female and male adults of Angiostrongylus cantonensis

Song, Zengmei; Huang, Huicong; Tan, Feng; Zhang, Erpeng; Hu, Jiayin; Pan, Chaoyun

doi:10.1016/j.exppara.2012.03.019

Cited by 12 publications

(11 citation statements)

References 17 publications

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“…The down-regulation of IDO, NEX1 annexin, and members of the TRRAP-like family observed in adult male A. cantonensis and the up-regulation observed in adult female A. cantonensis was coincidence with those published data. It may be related to the observation that female adults survived better than the male adults [47], [48]. However, these proteins were not found to be up-regulated in FL5 compared to ML5.…”

Section: Discussionmentioning

confidence: 96%

Development-Specific Differences in the Proteomics of Angiostrongylus cantonensis

et al. 2013

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Angiostrongyliasis is an emerging communicable disease. Several different hosts are required to complete the life cycle of Angiostrongylus cantonensis. However, we lack a complete understanding of variability of proteins across different developmental stages and their contribution to parasite survival and progression. In this study, we extracted soluble proteins from various stages of the A. cantonensis life cycle [female adults, male adults, the fifth-stage female larvae (FL5), the fifth-stage male larvae (ML5) and third-stage larvae (L3)], separated those proteins using two-dimensional difference gel electrophoresis (2D-DIGE) at pH 4–7, and analyzed the gel images using DeCyder 7.0 software. This proteomic analysis produced a total of 183 different dominant protein spots. Thirty-seven protein spots were found to have high confidence scores (>95%) by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). Comparative proteomic analyses revealed that 29 spots represented cytoskeleton-associated proteins and functional proteins. Eight spots were unnamed proteins. Twelve protein spots that were matched to the EST of different-stage larvae of A. cantonensis were identified. Two genes and the internal control 18s were chosen for quantitative real-time PCR (qPCR) and the qPCR results were consistent with those of the DIGE studies. These findings will provide a new basis for understanding the characteristics of growth and development of A. cantonensis and the host–parasite relationship. They may also assist searches for candidate proteins suitable for use in diagnostic assays and as drug targets for the control of eosinophilic meningitis caused by A. cantonensis.

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Section: Discussionmentioning

confidence: 96%

Development-Specific Differences in the Proteomics of Angiostrongylus cantonensis

et al. 2013

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“…In definitive hosts, L3 migrate to the central nervous system (CNS) and develop into the fourth- and the fifth-stage larvae (L4 and L5). The L5 then migrate to the pulmonary artery and heart of the definitive hosts via the circulatory system, where they develop into adult nematodes [ 2 – 4 ]. Humans, despite being unsuitable hosts, can become infected by drinking/eating water/food contaminated by L3 of A. cantonensis , leading to eosinophilic meningitis, eosinophilic encephalitis [ 3 – 5 ], and ocular angiostrongyliasis [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

“…Previously, by utilizing two-dimensional gel electrophoresis (2-DIGE) and mass spectrometry (MS), we found that several interesting proteins of A. cantonensis , including Gal-1 and PAS-5, could be strongly recognized by sera from mice infected with A. cantonensis [ 3 , 4 , 10 ]. PAS-5 is α5 proteasomal subunit and plays a major role in inducing host immune response [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

“…The proteasomes of parasites may alter the morphology of cells within the host, remove damaged and defunct proteins, and execute other functions to participate in the immune response [ 12 ]. Galectins are involved in various physiological and pathological processes, including RNA transcription, cell adhesion, cell apoptosis and immune regulation [ 3 , 4 , 13 ]. Of all galectin members, the most studied is Gal-1, which has been found to be involved in the regulation of the immune response [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

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The opposite roles of PAS-5 and Galectin-1 in immune response during the early infection of Angiostrongylus cantonensis

Yan

Shi

et al. 2018

Parasites Vectors

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BackgroundAngiostrongylus cantonensis is a human zoonotic nematode parasite. Our previous studies found that PAS-5 and Galectin-1 (Gal-1) proteins of A. cantonensis could be strongly recognized by sera from mice infected with A. cantonensis. In this study, we further evaluated the potential roles of these two proteins in the induction of immune response in mice.MethodsMice were immunized with recombinant PAS-5 or Gal-1 and then challenged with 30 infective A. cantonensis larvae following the last immunization. We then examined the infected mice for changes in serum antibodies and cytokines by ELISA, CD4+ T cells and CD4+CD25+FoxP3+ regulatory T cells (Tregs) by flow cytometry, and tissue damage severity by hematoxylin-eosin (H&E) staining.ResultsCompared with control mice, the PAS-5-immunized mice exhibited increased levels of serum antibodies and cytokines (except for IL-10) at different time points post-infection. PAS-5 immunization promoted significant proliferation of CD4+ T cells, and caused more damage in the brain tissue. Vaccination with Gal-1 inhibited the production of antibodies (except for IgG1) and IFN-γ, but promoted the expression of IL-4 and IL-10. Gal-1 immunization results in significant increases in the levels of CD4+CD25+FoxP3+ Tregs, and mild inflammatory changes.ConclusionsTaken together, our findings show that PAS-5 enhances, but Gal-1 inhibits the immune response in the early stage of A. cantonensis infections.

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“…In our previous study, using differential proteomics analysis of A. cantonensis at different stages of development, we showed that the expression level of A. cantonensis galectin (AcGal)-1 was higher in fifth-stage larvae (L5) than in third-stage larvae (L3) [7]. Galectins (Gals) constitute a family of lectins conserved across many species and are characterized by an affinity for β-galactoside and the presence of a conserved sequence motif known as the carbohydrate recognition domain (CRD) [8].…”

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confidence: 99%

Angiostrongylus cantonensis Galectin-1 interacts with Annexin A2 to impair the viability of macrophages via activating JNK pathway

et al. 2020

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Background: Angiostrongylus cantonensis can cause severe symptoms of central nervous system infections. In the host, this parasite localizes in the blood and cerebrospinal fluid, and its secreted components can impact immune responses. Our previous study demonstrated that immune responses were inhibited in A. cantonensis-infected mice immunized with Ac-Galectin-1 (AcGal-1). However, the mechanisms by which AcGal-1 regulates the immune responses remain unclear. Macrophages are innate immune cells that rapidly respond to infection. The direct impact of AcGal-1 on macrophages may affect the immune responses.Methods: AcGal-1 protein was purified by nickel ion affinity chromatography. The effect of AcGal-1 on the apoptosis of macrophages was detected using CCK-8 assay, flow cytometry and western blot. Macrophage membrane proteins bound to AcGal-1 were obtained using the His-tag-based pull-down assay and identified via mass spectrometry. Co-localization of AcGal-1 and the macrophage membrane protein Annexin A2 was observed by immunofluorescence microscopy, and their interaction was validated by co-immunoprecipitation experiments. SiRNA-mediated knockdown of Annexin A2 was used to determine if AcGal-1-induced macrophage apoptosis required interaction with Annexin A2. The phosphorylation level of apoptotic signal pathway protein was detected by phospho-antibody microarray and western blot. Results:Our study showed that AcGal-1 caused apoptosis of the macrophages. AcGal-1 increased the expression of apoptosis proteins caspase-3, caspase-9, Bax, but reduced the expression of anti-apoptosis protein Bcl-2. AcGal-1 interacted with the membrane protein Annexin A2, and knockdown of Annexin A2 expression increased Bcl-2 but decreased Bax levels in AcGal-1-treated cells. Moreover, AcGal-1 increased JNK phosphorylation and the inhibition of JNK phosphorylation in AcGal-1-treated cells decreased the expression of caspase-3, -9, Bax and almost restored Bcl-2 to the level observed in control cells. Conclusions:AcGal-1 can induce the apoptosis of macrophages by binding to Annexin A2 and activating JNK downstream the apoptotic signaling pathway.

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Differential proteomics analysis of female and male adults of Angiostrongylus cantonensis

Cited by 12 publications

References 17 publications

Development-Specific Differences in the Proteomics of Angiostrongylus cantonensis

Development-Specific Differences in the Proteomics of Angiostrongylus cantonensis

The opposite roles of PAS-5 and Galectin-1 in immune response during the early infection of Angiostrongylus cantonensis

Angiostrongylus cantonensis Galectin-1 interacts with Annexin A2 to impair the viability of macrophages via activating JNK pathway

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