intestinal volvulus/protease

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Onchocerca volvulus: expression and immunolocalization of a nematode cathepsin D-like lysosomal aspartic protease.

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The N-terminal region of the cathepsin D-like aspartic protease from the human filarial parasite Onchocerca volvulus was expressed as His-tag fusion protein. Light and electron microscopic immunohistology using antibodies against the recombinant protein showed labeling of lysosomes in the hypodermis

Wolbachia endosymbionts of Onchocerca volvulus express a putative periplasmic HtrA-type serine protease.

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Wolbachia are intracellular bacteria of many filarial nematodes. A mutualistic interaction between the endobacteria and the filarial host is likely, because the clearance of Wolbachia by tetracycline leads to the obstruction of embryogenesis and larval development. Databases were searched for

Preliminary characterisation of an Onchocerca volvulus aspartic protease.

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PCR using 1 primer specific for aspartic proteases and 1 primer annealing to the vector allowed amplification of a 377 bp fragment encoding part of an aspartic protease from an Onchocerca volvulus cDNA library. Use of this fragment as a probe allowed the isolation of a larger cDNA clone. In common

Characterization of a novel filarial serine protease inhibitor, Ov-SPI-1, from Onchocerca volvulus, with potential multifunctional roles during development of the parasite.

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A novel filarial serine protease inhibitor (SPI) from the human parasitic nematode Onchocerca volvulus, Ov-SPI-1, was identified through the analysis of a molting third-stage larvae expressed sequence tag dataset. Subsequent analysis of the expressed sequence tag datasets of O. volvulus and other

RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting.

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We describe the successful use of RNA interference (RNAi) to investigate gene function in the human filarial parasite Onchocerca volvulus third-stage larvae (L3). We targeted two specific gene products, the O. volvulus cathepsin L (Ov-CPL) and cathepsin Z-like (Ov-CPZ) cysteine proteases, which were

Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae.

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We have investigated the involvement of a cysteine protease in the development of Onchocerca volvulus fourth stage larvae (L4) by testing the effect of cysteine protease inhibitors on the survival of third stage larvae (L3), and the molting of L3 to L4 in vitro. When larvae were cultured in the

A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling.

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Cysteine proteinases are involved in a variety of important biological processes and have been implicated in molting and tissue remodeling in free living and parasitic nematodes. We show that in the lymphatic filarial nematode Brugia pahangi molting of third-stage larvae (L3) to fourth-stage larvae

Onchocerca volvulus: microfilariae secrete elastinolytic and males nonelastinolytic matrix-degrading serine and metalloproteases.

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Host tissue penetration by parasitic nematodes may be mediated by both mechanical processes and proteolytic enzymes released by the parasites. Analysis of excretory-secretory (ES) products of Onchocerca volvulus microfilariae and adult stages on substrate gels demonstrated that they contain several

Effects of an Onchocerca-derived cysteine protease inhibitor on microfilariae in their simuliid vector.

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A recombinant cysteine protease inhibitor, onchocystatin of the parasitic nematode Onchocerca volvulus, was tested for its role in microfilarial development in the simuliid vector. Onchocystatin was found to be present in female adults and skin microfilariae of the bovine parasite O. ochengi, the

[Proteolytic activity of adult worm extracts of Onchocerca volvulus].

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Studying proteolytic activity of Onchocerca volvulus (nematode causing "river blindness") shows that it is able to digest a variety of substrates such as: azoalbumine, azocoll and elastin-orcein with specific activity of 0.28, 0.57 and 1.48 mg/hour/mg of extract respectively. These enzymes are

Cloning and biochemical characterization of blisterase, a subtilisin-like convertase from the filarial parasite, Onchocerca volvulus.

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Blisterase is a subtilisin-like proprotein convertase of nematodes. The enzyme is named after the blistered cuticle found in Caenorhabditis elegans with the bli-4 e937 mutation. The critical role of the enzyme in cuticle production makes it a potential drug target for parasitic nematodes. We have

Pathogenesis of onchocercal dermatitis: possible role of parasite proteases and autoantibodies to extracellular matrix proteins.

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We examined the immunogenicity of various connective tissue proteins in patients with chronic onchocercal dermatitis and the effect of filarial proteases on this host-parasite interaction. Sera from patients with onchocerciasis reacted strongly with cuticular collagens from filarial parasites and

Identification of a novel family of non-lysosomal aspartic proteases in nematodes.

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A protein encoded by cDNAs from the human parasite Onchocerca volvulus and its homologs from Caenorhabditis elegans and Ancyclostoma caninum define a family of aspartic proteases that are most closely related to cathepsins D, but differ from them in lacking the N-glycosylation site known to be

Identification and characterization of onchoastacin, an astacin-like metalloproteinase from the filaria Onchocerca volvulus.

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The tissue-invasive nematode Onchocerca volvulus causes skin and eye pathology in human onchocerciasis. While the adult females reside sessile in subcutaneous nodules, the microfilariae are abundantly released from the nodules, males and juvenile worms migrate through the host tissue.

Onchocerca volvulus, O. gutturosa, Brugia malayi, and Dirofilaria immitis: a comparative study of the immunochemical properties of cuticular proteins from filarial parasites.

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We compared the chemical and immunological properties of cuticular collagens from four species of filarial nematodes, Onchocerca volvulus, O. gutturosa, Brugia malayi, and Dirofilaria immitis. The electrophoretic mobility of the major polypeptides extracted from adult worms is characteristic for

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