A cathepsin L-like cysteine proteinase gene from the protozoan parasite, Cryptobia salmositica

Jesudhasan, Palmy R.; Tan, Chung-Wei; Hontzeas, Nikos; Woo, P. T. K.

doi:10.1007/s00436-006-0344-3

Cited by 12 publications

(3 citation statements)

References 24 publications

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“…The characteristics of the peptidase proteins, including frequency, protein length, homology to previously deposited proteins and conserved domains are shown in Table 1. The conserved domains were analyzed using the SMART web program, Genbank BLAST program, and other literature [16-22]. …”

Section: Resultsmentioning

confidence: 99%

Molecular cloning and expression analysis of peptidase genes in the fish-pathogenic scuticociliate Miamiensis avidus

et al. 2013

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BackgroundParasite peptidases have been actively studied as vaccine candidates or drug targets for prevention or treatment of parasitic diseases because of their important roles for survival and/or invasion in the host. Like other parasites, the facultative histophagous ciliate Miamiensis avidus would possess peptidases that are closely associated with the invasion into the host tissue and survival in the host.ResultsThe 17 genes encoding peptidases, including seven cathepsin-like cysteine peptidases, four serine carboxypeptidases, a eukaryotic aspartyl protease family protein, an ATP-dependent metalloprotease FtsH family protein, three leishmanolysin family proteins and a peptidase family M49 protein were identified from a Miamiensis avidus cDNA library by BLAST X search. Expression of genes encoding two cysteine peptidases, three leishmanolysin-like peptidases and a peptidase family M49 protein was up-regulated in the cell-fed ciliates compared to the starved ciliates. Especially, one cysteine peptidase (MaPro 4) and one leishmanolysin-like peptidase (MaPro 14) were transcribed more than 100-folds in the cell-fed ciliates.ConclusionsThe genetic information and transcriptional characteristics of the peptidases in the present results would be helpful to elucidate the role of peptidases in the invasion of scuticociliates into their hosts.

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Section: Resultsmentioning

confidence: 99%

Molecular cloning and expression analysis of peptidase genes in the fish-pathogenic scuticociliate Miamiensis avidus

et al. 2013

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“…and Trypanosoma spp. (Jesudhasan et al 2007a), while the metallopeptidase was shown to share homology with the major surface metallopeptidase from Leishmania spp. (Jesudhasan et al 2007b).…”

Section: Discussionmentioning

confidence: 99%

Bodo sp., a Free‐Living Flagellate, Expresses Divergent Proteolytic Activities from the Closely Related Parasitic Trypanosomatids

d’Avila-Levy

Volotão

Araújo

et al. 2009

J Eukaryotic Microbiology

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We report the characterization of cell-associated and extracellular peptidases of Bodo sp., a free-living flagellate of the Bodonidae family, order Kinetoplastida, which is considered ancestral to the trypanosomatids. This bodonid isolate is phylogenetically related to Bodo caudatus and Bodo curvifilus. The proteolytic activity profiles of Bodo sp. were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis containing co-polymerized gelatin, casein, hemoglobin, or bovine serum albumin as substrates. The enzymatic complex degraded gelatin better in acidic pH, and under these conditions four proteolytic bands (120, 100, 90, and 75 kDa) were detected in the cellular or extracellular extracts. Two peptidases (250 and 200 kDa) were exclusively detected with the substrate casein. All these enzymes belong to the serine peptidase class, based on inhibition by aprotinin and phenylmethylsulfonyl fluoride. This is the first biochemical characterization of peptidases in a free-living Bodo sp., potentially providing insight into the physiology of these protozoa and the evolutionary importance of peptidases to the order Kinetoplastida as some of these enzymes are important virulence factors in pathogenic trypanosomatids.

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“…Briefly, the metalloprotease and cysteine protease genes of C. salmositica were sequenced [45, 46] and inserted into plasmid vectors (pEGFP-N) to produce a metalloprotease-plasmid vaccine and a cysteine-plasmid vaccine [47]. Rainbow trout and Atlantic salmon, Salmo salar , injected intramuscularly with the metalloprotease-plasmid vaccine consistently had lower packed cell volume (as metalloprotease was secreted into the blood) than controls (fish inoculated either with plasmid alone or with cysteine-plasmid vaccine) at 2–4 wpv.…”

Section: Strategies Against Cryptobia and Cryptobiosismentioning

confidence: 99%

Immunological and Therapeutic Strategies against Salmonid Cryptobiosis

Woo

2010

Journal of Biomedicine and Biotechnology

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Salmonid cryptobiosis is caused by the haemoflagellate, Cryptobia salmositica. Clinical signs of the disease in salmon (Oncorhynchus spp.) include exophthalmia, general oedema, abdominal distension with ascites, anaemia, and anorexia. The disease-causing factor is a metalloprotease and the monoclonal antibody (mAb-001) against it is therapeutic. MAb-001 does not fix complement but agglutinates the parasite. Some brook charr, Salvelinus fontinalis cannot be infected (Cryptobia-resistant); this resistance is controlled by a dominant Mendelian locus and is inherited. In Cryptobia-resistant charr the pathogen is lysed via the Alternative Pathway of Complement Activation. However, some charr can be infected and they have high parasitaemias with no disease (Cryptobia-tolerant). In infected Cryptobia-tolerant charr the metalloprotease is neutralized by a natural antiprotease, α2 macroglobulin. Two vaccines have been developed. A single dose of the attenuated vaccine protects 100% of salmonids (juveniles and adults) for at least 24 months. Complement fixing antibody production and cell-mediated response in vaccinated fish rise significantly after challenge. Fish injected with the DNA vaccine initially have slight anaemias but they recover and have agglutinating antibodies. On challenge, DNA-vaccinated fish have lower parasitaemias, delayed peak parasitaemias and faster recoveries. Isometamidium chloride is therapeutic against the pathogen and its effectiveness is increased after conjugation to antibodies.

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A cathepsin L-like cysteine proteinase gene from the protozoan parasite, Cryptobia salmositica

Cited by 12 publications

References 24 publications

Molecular cloning and expression analysis of peptidase genes in the fish-pathogenic scuticociliate Miamiensis avidus

Molecular cloning and expression analysis of peptidase genes in the fish-pathogenic scuticociliate Miamiensis avidus

Bodo sp., a Free‐Living Flagellate, Expresses Divergent Proteolytic Activities from the Closely Related Parasitic Trypanosomatids

Immunological and Therapeutic Strategies against Salmonid Cryptobiosis

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