Sequence, characterization and localization of a cysteine proteinase cathepsin L in Schistosoma mansoni

Michel, Anja; Ghoneim, Hossam; Resto, Maristella; Klinkert, Mo‐Quen; Kunz, Werner

doi:10.1016/0166-6851(95)00092-f

Cited by 54 publications

(36 citation statements)

References 38 publications

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“…Cysteine proteinases from some trematodes were reported to localize in the intestine or in cercarial extracts or immature eggs (10,13,20), but immnocytochemical analysis of C. sinensis cysteine proteinases has not been reported. In this study, C. sinensis cysteine proteinases are localized in the intestinal epithelial cells of the adult parasite and in the intrauterine eggs.…”

Section: Discussionmentioning

confidence: 99%

Molecular Expression of a Cysteine Proteinase of Clonorchis sinensis and Its Application to an Enzyme-Linked Immunosorbent Assay for Immunodiagnosis of Clonorchiasis

Nagano

Pei

et al. 2004

Clin Vaccine Immunol

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We produced a recombinant cysteine proteinase of Clonorchis sinensis and tested its value as an antigen for serologic diagnosis of C. sinensis infections. The predicted amino acid sequence of the cysteine proteinase of C. sinensis was 58, 48, and 40% identical to those of cathepsin L cysteine proteinases from Paragonimus westermani, Schistosoma japonicum, and Fasciola hepatica, respectively. Western blotting analysis showed that sera from patients infected with C. sinensis strongly reacted with the recombinant protein and that sera from patients infected with S. japonicum weakly reacted with the recombinant protein. Antibody against the recombinant protein stained proteins migrating at about 37 and 28 kDa in C. sinensis adult worm crude extracts. Immunostaining revealed that the cysteine proteinase of C. sinensis was located in the intestinal epithelial cells of the adult parasite and in intrauterine eggs. The specificity and sensitivity of the recombinant antigen or C. sinensis adult worm crude extracts were assessed by an enzyme-linked immunosorbent assay (ELISA) using serum samples from humans infected with different parasites, including 50 patients with clonorchiasis, and negative controls. The sensitivities of the ELISA with the recombinant antigen and C. sinensis adult worm crude extracts were 96 and 88%, respectively. The specificities of the ELISA with the recombinant antigen and C. sinensis adult worm crude extracts were 96.2 and 100%, respectively. The results suggested that the recombinant cysteine proteinase-based ELISA could provide a highly sensitive and specific assay for diagnosis of clonorchiasis.

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Section: Discussionmentioning

confidence: 99%

Molecular Expression of a Cysteine Proteinase of Clonorchis sinensis and Its Application to an Enzyme-Linked Immunosorbent Assay for Immunodiagnosis of Clonorchiasis

Nagano

Pei

et al. 2004

Clin Vaccine Immunol

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“…Considering these observations and the fact that cathepsin B and asparaginyl endopeptidases also function internally within cells (42,43), it is likely that these newly discovered proteases have functions within the internal tissues of this complex multicellular parasite and are involved in generalized protein turnover, remodeling, and/or catabolism. Alternatively or additionally, because immunocytochemistry and in situ hybridization have localized cysteine proteases and transcripts to the reproductive structures of other trematodes (44,45) these proteases may be involved in the process of egg production. Other proteins identified by EST2Secretome analysis but not by proteomics, including the previously uncharacterized proteins such as deoxyribonucleases, carboxypeptidase, and trypsin-like peptidases that have homologues in Schistosoma japonicum and C. sinensis, may also be confined to internal tissues of the parasite or be expressed and secreted at levels below the detection capacity of the proteomics methods so far used (cDNAs of these were poorly represented in the transcriptome of the adult parasite).…”

Section: Discussionmentioning

confidence: 99%

An Integrated Transcriptomics and Proteomics Analysis of the Secretome of the Helminth Pathogen Fasciola hepatica

Robinson

Menon

Donnelly

et al. 2009

Molecular & Cellular Proteomics

248

249

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To infect their mammalian hosts, Fasciola hepatica larvae must penetrate and traverse the intestinal wall of the duodenum, move through the peritoneum, and penetrate the liver. After migrating through and feeding on the liver, causing extensive tissue damage, the parasites move to their final niche in the bile ducts where they mature and produce eggs. Here we integrated a transcriptomics and proteomics approach to profile Fasciola secretory proteins that are involved in host-pathogen interactions and to correlate changes in their expression with the migration of the parasite. Prediction of F. hepatica secretory proteins from 14,031 expressed sequence tags (ESTs) available from the Wellcome Trust Sanger Centre using the semiautomated EST2Secretome pipeline showed that the major components of adult parasite secretions are proteolytic enzymes including cathepsin L, cathepsin B, and asparaginyl endopeptidase cysteine proteases as well as novel trypsinlike serine proteases and carboxypeptidases. Proteomics analysis of proteins secreted by infective larvae, immature flukes, and adult F. hepatica showed that these proteases are developmentally regulated and correlate with the passage of the parasite through host tissues and its encounters with different host macromolecules. Proteases such as FhCL3 and cathepsin B have specific functions in larvae activation and intestinal wall penetration, whereas FhCL1, FhCL2, and FhCL5 are required for liver penetration and tissue and blood feeding. Besides proteases, the parasites secrete an array of antioxidants that are also highly regulated according to their migration through host tissues. However, whereas the proteases of F. hepatica are secreted into the parasite gut via a classical endoplasmic reticulum/Golgi pathway, we speculate that the antioxidants, which all lack a signal sequence, are released via a non-classical trans-tegumental pathway. Fasciola hepatica is a helminth (worm) parasite with a worldwide distribution. Although traditionally regarded as a parasite of livestock, particularly sheep and cattle, that results in a large economic loss to the agricultural community it has recently emerged as an important human infection in many regions of the world, including South America, Iran, Egypt, and mainland South-East Asia (1). Dormant larvae contained within cysts adhere to vegetation and emerge as infective juveniles (newly excysted juveniles (NEJs)) 1 in the duodenum following ingestion by animals or humans. They infect their hosts by rapidly penetrating the intestinal wall and entering the peritoneal cavity where they break through the liver capsule. After 8 -12 weeks of consistent burrowing, feeding, and growth within the liver parenchyma they move to their final destination within the bile ducts where they mature and produce enormous numbers of eggs (2). The two distinct clinical phases of fasciolosis are directly related to the migration of the parasites: acute fasciolosis, which manifests as fever, abdominal pain, weight loss, and hepatomegaly, is associated with...

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“…From several known cathepsin L (isolated in Fasciola hepatica, Schistosoma mansoni and Drosophila melanogaster), degenerated primers were designated to amplify several regions of cathepsin L cDNA by RT-PCR [11,18,19]. Internal, 5′ end and 3′ end products were necessary to obtain a full length cDNA corresponding to T. tessulatum preprocathepsin L gene, named Tt-catl (Accession number Q8IT42 in the UniProt server of the European Bioinformatics Institute) (Fig.…”

Section: Theromyzon Tessulatum Cathepsin L (Tt-catl) Characterizationmentioning

confidence: 99%

Cathepsin L and cystatin B gene expression discriminates immune cœlomic cells in the leech Theromyzon tessulatum

Lefebvre

Vandenbulcke

Bocquet

et al. 2008

Developmental & Comparative Immunology

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Previous studies evidenced that cystatin B-like gene is specifically expressed and induced in large circulating coelomic cells following bacterial challenge in the leech Theromyzon tessulatum. In order to understand the role of that cysteine proteinase inhibitor during immune response, we investigated the existence of members of cathepsin family. We cloned a cathepsin L-like gene and studied its tissue distribution. Immunohistochemical studies using anti-cathepsin L and anti-cystatin B antibodies and ultrastructural results demonstrated the presence of three distinct coelomic cell populations, (1) the chloragocytes which were initially defined as large coelomocytes, (2) the granular amoebocytes, and (3) small coelomic cells. Among those cells, while chloragocytes contain cystatin B and cathepsin L, granular amoebocytes do only contain cathepsin L and third cell population contains neither cathepsin nor inhibitor. Finally, results evidenced that cathepsin L immunopositive granular amoebocytes are chemoattracted to the site of injury and phagocyte bacteria.

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Sequence, characterization and localization of a cysteine proteinase cathepsin L in Schistosoma mansoni

Cited by 54 publications

References 38 publications

Molecular Expression of a Cysteine Proteinase of Clonorchis sinensis and Its Application to an Enzyme-Linked Immunosorbent Assay for Immunodiagnosis of Clonorchiasis

Molecular Expression of a Cysteine Proteinase of Clonorchis sinensis and Its Application to an Enzyme-Linked Immunosorbent Assay for Immunodiagnosis of Clonorchiasis

An Integrated Transcriptomics and Proteomics Analysis of the Secretome of the Helminth Pathogen Fasciola hepatica

Cathepsin L and cystatin B gene expression discriminates immune cœlomic cells in the leech Theromyzon tessulatum

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