ArticleParasitology research2011
Molecular cloning and characterization of a cathepsin B from Angiostrongylus cantonensis.
Article in Parasitology research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Cysteine proteases as digestive enzymes in parasitic helminths.PLoS neglected tropical diseases · 2018Review
- Nitric oxide and cytokine production by glial cells exposed in vitro to neuropathogenic schistosome Trichobilharzia regenti.Parasites & vectors · 2016Article
- Cloning and expression of a 16-kDa recombinant protein from Angiostrongylus cantonensis for use in immunoblot diagnosis of human angiostrongyliasis.Parasitology research · 2016Article
- Pepsin is a positive regulator of Ac-cathB-2 involved in the rat gut penetration of Angiostrongylus cantonensis.Parasites & vectors · 2016Article
- The cathepsin S cysteine proteinase of the burrowing nematode Radopholus similis is essential for the reproduction and invasion.Cell & bioscience · 2016Article
- Identification and characterization of Clonorchis sinensis cathepsin B proteases in the pathogenesis of clonorchiasis.Parasites & vectors · 2015Article
- Cathepsin B Cysteine Proteinase is Essential for the Development and Pathogenesis of the Plant Parasitic Nematode Radopholus similis.International journal of biological sciences · 2015Article
- Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration.Parasite (Paris, France) · 2015Article
- Novel cathepsin B and cathepsin B-like cysteine protease of Naegleria fowleri excretory-secretory proteins and their biochemical properties.Parasitology research · 2014Article
- Identification and characterization of an asparaginyl endopeptidase from Angiostrongylus cantonensis.Parasitology research · 2014Article
- Analysis of a novel cathepsin B circulating antigen and its response to drug treatment in Trichinella-infected mice.Parasitology research · 2013Article
- Identification and characterisation of microRNAs in young adults of Angiostrongylus cantonensis via a deep-sequencing approach.Memorias do Instituto Oswaldo Cruz · 2013Article
- Molecular characterization and immunolocalization of a protein disulfide isomerase from Angiostrongylus cantonensis.Parasitology research · 2012Article
- Molecular characterization and expression of a cysteine protease from Clonorchis sinensis and its application for serodiagnosis of clonorchiasis.Parasitology research · 2012Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine proteases, a superfamily of hydrolytic enzymes, have numerous functions in parasites. Here, we reported the cloning and characterization of a cDNA encoding a cathepsin B (AcCPB) from Angiostrongylus cantonensis fourth-stage larvae cDNA library. The deduced amino acid sequence analysis indicated AcCPB is related to other cathepsin B family members with an overall conserved architecture. AcCPB is evolutionarily more close to other parasitic nematode cathepsin B than the ones from hosts, sharing 43-53% similarities to the homologues from other organisms. Real-time quantitative PCR analysis revealed that AcCPB was expressed significantly higher in the fourth-stage larvae (L4) and the fifth-stage larvae (L5) than that in the third-stage larvae (L3) and adult worms (Aw). Unexpectedly, AcCPB was expressed at a higher level in L4 and L5 derived from mice than the larvae at the same stages derived from rats. The protease activity of recombinant AcCPB (rAcCPB) expressed in Escherichia coli showed high thermostability and acidic pH optima. The role in ovalbumin digestion and enzyme activity of rAcCPB could be evidently inhibited by cystatin from A.cantonensis. Furthermore, we found rAcCPB increased the expression levels of CD40, MHC II, and CD80 on LPS-stimulated dendritic cells (DCs). In this study, we provided the first experimental evidence for the expression of cathepsin B in A.cantonensis. Besides its highly specific expression in the stages of L4 and L5 when the worms cause dysfunction of the blood-brain barrier of hosts, AcCPB displayed different expression profiles in non-permissive host- and permissive host-derived larval stages and was involved in the maturation of DCs, suggesting a potential role in the central nervous system invasion and the immunoregulation during parasite-host interactions.
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