ArticleParasites & vectors2020
Angiostrongylus cantonensis Galectin-1 interacts with Annexin A2 to impair the viability of macrophages via activating JNK pathway.
Article in Parasites & vectors, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Trichinella spiralis galectin disrupts gut epithelial integrity and mediates larval invasion via acting MUC13- ROCK2/MAPK pathway.PLoS neglected tropical diseases · 2026Article
- Proteomic profiles of Lissachatina (Heterobranchia) and Pomacea (Caenogastropoda) snails infected with Angiostrongylus cantonensis using 4D label-free quantitative analysis.PLoS neglected tropical diseases · 2025Article
- Modulation of the Immune Response by Nematode Derived Molecules.International journal of molecular sciences · 2025Review
- Isolate-specific rat brain transcriptional responses to rat lungworm (Angiostrongylus cantonensis).Pathogens and disease · 2025Article
- Extracellular vesicles from fifth-stage larvalmSystems · 2025Article
- Knockdown of annexin A2 enhances the host cell apoptosis induced byFrontiers in veterinary science · 2025Article
- Identification and Immunological Characterization of Annexin B8 and Annexin E1 from Spirometra Erinaceieuropaei Spargana.Parasitology research · 2024Article
- Nematode Galectin Inhibits Basophilic Leukaemia RBL-2H3 Cells Apoptosis in IgE-Mediated Activation.International journal of molecular sciences · 2024Article
- A novel Trichinella spiralis serine proteinase disrupted gut epithelial barrier and mediated larval invasion through binding to RACK1 and activating MAPK/ERK1/2 pathway.PLoS neglected tropical diseases · 2024Article
- Annexin gene family in Spirometra mansoni (Cestoda: Diphyllobothriidae) and its phylogenetic pattern among Platyhelminthes of medical interest.Parasite (Paris, France) · 2024Article
- Review
- The Impact of Intestinal Inflammation on Nematode's Excretory-Secretory Proteome.International journal of molecular sciences · 2023Article
- Galectin-1: A Traditionally Immunosuppressive Protein Displays Context-Dependent Capacities.International journal of molecular sciences · 2023Review
- Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasiteFrontiers in cellular and infection microbiology · 2023Article
- Characterization of a novel galectin inFrontiers in microbiology · 2023Article
- Upregulated galectin-1 in Angiostrongylus cantonensis L5 reduces body fat and increases oxidative stress tolerance.Parasites & vectors · 2022Article
- The interaction of host and nematode galectins influences the outcome of gastrointestinal nematode infections.Parasitology · 2021Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundAngiostrongylus 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.
methodsAcGal-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.
resultsOur 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.
conclusionsAcGal-1 can induce the apoptosis of macrophages by binding to Annexin A2 and activating JNK downstream the apoptotic signaling pathway.
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