Proteolytic enzymes secreted by larval stage of the parasitic nematode Trichinella spiralis.
Excretory/secretory products (ES), collected from in vitro cultures of muscle larvae (L1) of Trichinella spiralis (Owen, 1835) were examined for the presence of proteolytic enzymes. Several discrete proteinases in the size range of 25-55 kDa were identified by substrate gel electrophoresis and were characterised according to pH optima, substrate specificity and inhibitor sensitivity using azocasein assay. Serine, cysteine and metalloproteinases active at pH 5-7 were identified. The serine proteinases were found to predominate and some of them were found to be specific for the larval stage of the parasite. The results from the substrate analysis indicated the presence of collagenolytic and elastolytic activities. The proteinase activity was inhibited by IgG isolated from T. spiralis-infected mice, an observation of relevance to understanding host/parasite interactions and, ultimately, the development of anti-Trichinella vaccine.
Todorova
V K
VK
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia. vtodorov@obzor.bio21.bas.bg
D000818:Animals; D000909:Antibodies, Helminth / Q000097:blood / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000201:enzymology / Q000254:growth & development; D051379:Mice; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D017160:Trichinella spiralis / Q000201:enzymology* / Q000254:growth & development; D014235:Trichinellosis / Q000469:parasitology*
D000909:Antibodies, Helminth; D011480:Protease Inhibitors; D010450:Endopeptidases