Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A peanut agglutinin-binding glycoprotein in adult Schistosoma mansoni was shown to be absent from pre-liver worms, but could be detected on the worm surface in large amounts at four weeks post-infection. Four-week parasites incubated with fluorescein isothiocyanate-peanut agglutinin showed a general surface fluorescence. The molecule did not incorporate methionine or palmitate. ELISA using the isolated glycoprotein showed the presence of antibodies to it in serum from infected mice and from humans infected with S. mansoni and Schistosoma haematobium. The implications of these results for surface membrane development are discussed.
Mol Biochem Parasitol 1989 May 15
PMID:Isolation and characterisation of a surface membrane glycoprotein from adult Schistosoma mansoni. 273 29

Adult Fasciola hepatica worms contain multiple proteinases capable of degrading hemoglobin, immunoglobulins and collagen. Here we report the isolation and biochemical characterization of a cysteine proteinase from acidic extracts of these worms. The enzyme was purified to homogeneity by cation exchange and molecular sieve high-performance liquid chromatography. It eluted at a native molecular weight of approximately 14,500 and migrated as a single band at approximately 14,500 Da upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Activity was assessed by employing synthetic peptide substrates, such as carbobenzoxy-phenylalanyl-arginyl-7-amino-4-trifluoro-methylcoumarin, commonly used to assay other cysteine proteinases. The proteinase was maximally active at pH 6.0, with 50% or more of the activity detected between pH 4.5 and 7.5. Inhibition of activity at pH 5.5 was seen only with compounds known to inhibit cysteine proteinases. No effect was seen with inhibitors of aspartic, serine, or metalloproteinases. The purified enzyme was stable at acidic pH at 4 degrees C, 25 degrees C, -20 degrees C, and in 1 M urea.
Mol Biochem Parasitol 1989 Jun 01
PMID:Isolation and characterization of a cysteine proteinase from Fasciola hepatica adult worms. 276 75

This report describes a method for the identification of the sex of Schistosoma mansoni cercariae using a cloned DNA probe which is female-specific. The probe is a 339 bp repeat; the sequence is presented. Cercariae from nine mono-miracidially infected snails were used in a double blind study. Mice were infected and the sex of adult worms observed. DNA was isolated from cercariae, digested with EcoRI, subjected to agarose gel electrophoresis, transferred to a matrix and hybridized with the cloned female-specific DNA probe. In all nine cases the sex of the cercariae as determined by DNA analysis agreed with the sex of the adult parasites.
Mol Biochem Parasitol 1987 Nov
PMID:A cloned DNA probe identifies the sex of Schistosoma mansoni cercariae. 282 46

The turnover of surface proteins in adults, fourth-stage and third-stage larvae of Brugia pahangi was measured using [125I]iodosulfanilic acid. Groups of worms (n = 10 adult, 20 L4, 50 L3) were labelled and surgically implanted into the peritoneal cavity of naive jirds. The amount of radioactivity remaining on worms recovered over a 7-8 day period was determined. Adult females showed no significant loss of label during a 7 day period. The recovery of fourth-stage larvae was low but the counts per minute remaining on each group of larvae recovered over an 8 day period, encompassing the major part of the instar, did not fall below the limits of the standard deviation of the time 0 groups, indicating that no significant loss of surface label had occurred. Third-stage larvae showed a significant loss of 125I-labelled proteins prior to the third moult, although it was not confirmed that these proteins occur on the worm surface. Electrophoresis and autoradiography of labelled homogenates of adult, fourth and third stage larvae suggested that [125I]iodosulfanilic acid labels polypeptides of different molecular weights on each life cycle stage of B. pahangi.
Mol Biochem Parasitol 1986 Jan
PMID:Turnover of the surface proteins of adult and third and fourth stage larval Brugia pahangi. 287 Apr 32

A previously described cDNA clone, pSF10, of Schistosoma mansoni encoding the very dominant female specific polypeptide (FSP) has been used to characterize the gene and its expression. The gene is detectable in different isolates of S. mansoni and is estimated to be present in 3 copies per haploid genome. The gene is not sex linked and exhibits neither amplification nor rearrangement concomitant with expression. Expression of the gene by parasites maturing in hamsters is first detected after 5 weeks when the RNA is present at 1/10 the level of that of 6 week worms. Although the FSP gene is specifically and highly expressed by egg laying female worms a corresponding polypeptide produced by the cell-free translation of RNA is not detectable. It was confirmed, however, that pSF10 does indeed encode a mRNA by DNA sequence analysis. The sequence demonstrated a mRNA containing a poly(A) tail and two open reading frames. One reading contains no methionine but is very high (47%) in glycine. This amino acid composition could account for the inability to detect the gene product by cell-free translation in the presence of [35S]methionine.
Mol Biochem Parasitol 1987 Jan 15
PMID:Characterisation of the structure and expression of the gene encoding a major female specific polypeptide of Schistosoma mansoni. 288 71

To understand mechanisms involved in sex-specific gene expression in Schistosoma mansoni, a cDNA (fs800) was isolated that hybridized to an 800 nucleotide mRNA present in high levels only in mature female worms. The fs800 cDNA sequence was characterized by two long open reading frames and central stretches of repeated amino acids. Fs800 did not share similarities with other known sequences in computer searches. In situ hybridization, however, revealed that the mRNA corresponding to fs800 was found only in female vitelline cells, suggesting that the product of this gene may be involved in the production or function of eggs. Fs800 is developmentally regulated as expression of this gene is dependent on the maturity of female worms. Furthermore, during in vitro culture, when female worms are known to stop egg production, expression of fs800 selectively ceased.
Mol Biochem Parasitol 1989 Jan 15
PMID:Localization and pattern of expression of a female specific mRNA in Schistosoma mansoni. 292 41

The major structural proteins of the cuticle of the filarial nematode parasites Brugia malayi and Brugia pahangi were identified by extrinsic iodination and sensitivity to clostridial collagenase. At least 16 acidic components were identified in adult worms by 2-dimensional electrophoresis, with molecular weights ranging from 35,000 to 160,000. These proteins appear to be cross-linked by disulphide bonds, and localised in the basal and inner cortical layers of the cuticle. The outer cortex, containing the epicuticle, is insoluble in 1% sodium dodecyl sulphate and 5% 2-mercaptoethanol, and can be isolated free of cellular material. Despite their inaccessibility to the immune system in intact worms, antibodies to the cuticular collagens are provoked in humans infected with a variety of filarial parasites. Immunological cross-reactivity was demonstrated between a 35 kDa component and human type IV (basement membrane) collagen. Autoantibodies to type IV collagen were detected in a number of individuals with lymphatic filariasis, although no correlation could be drawn with observed pathology. Synthesis of cuticular collagens is discontinuous, occurs at negligible levels in mature adult male worms, and does not appear to involve the production of small molecular weight precursors, in contrast to Caenorhabditis elegans. Hybridisation with a heterologous cDNA probe coding for the alpha 2 chain of chicken type 1 collagen suggests that they are encoded by a multigene family.
Mol Biochem Parasitol 1989 Jan 15
PMID:Identification, synthesis and immunogenicity of cuticular collagens from the filarial nematodes Brugia malayi and Brugia pahangi. 292 47

A cDNA library was constructed from the mRNA of adult worms of Schistosoma mansoni, in the expression vector lambda gt11. This library was screened with a pool of sera raised against either soluble egg antigens or purified schistosomulum tegumental membranes. An antiserum raised against the fusion protein of one clone immunoprecipitated a 45 kDa polypeptide from the in vitro translation products of adult worm mRNA and recognised a 50 kDa antigen in homogenates of adult worms. This serum gave positive fluorescence of the surface of schistosomula in indirect immunofluorescence assays and was able to mediate killing of schistosomula by human eosinophils in vitro, suggesting that this clone contained part of a gene encoding a surface antigen.
Mol Biochem Parasitol 1988 Jul
PMID:Cloning of the gene encoding a 50 kilodalton potential surface antigen of Schistosoma mansoni. 296 55

The presence of 5'-nucleotidase was demonstrated in Onchocerca volvulus and Dirofilaria immitis; the bulk of activity was found in the particulate fraction. The enzyme of filarial worms exhibited a broad pH-optimum between 6.4 and 8.0 and substrate specificity for nucleotides compared to glucose-6-phosphate and p-nitrophenyl phosphate. The apparent Km-values for AMP were found to be 0.15 mM and 0.22 mM for the enzyme from O. volvulus and D. immitis, respectively. The activity of 5'-nucleotidase from both filarial worms was effectively inhibited by the filaricidal compound CGP 8065, a dithiocarbamate-derivative of amoscanate, whereas the 5'-nucleotidase from rat liver was not affected. The parasite-specific inhibition by CGP 8065 was found to be reversible and to be competitive with respect to the substrate AMP. The inhibition constants were calculated to be 24 microM and 8 microM for the enzyme from O. volvulus and D. immitis, respectively.
Mol Biochem Parasitol 1985 Aug
PMID:Parasite-specific inhibition of 5'-nucleotidase from Onchocerca volvulus and Dirofilaria immitis by the amoscanate-derivative CGP 8065. 299 82

A library of randomly sheared Schistosoma japonicum genomic DNA fragments was constructed in the bacteriophage expression vector lambda gt11. A portion of the library was screened with sera collected from rabbits 8 weeks after they were infected with 1000 cercariae. Four clones whose recombinant gene products react with the rabbit sera were purified to homogeneity. Clone SjIR-12A was chosen for detailed study because of its very intense reaction with the rabbit sera. SjIR-12A was found to encode part of a 70 kDa protein (Sj70) that is present in both soluble egg antigen (SEA) and soluble worm antigen preparations (SWAP). Western blot analysis suggests that Sj70 is the only SWAP component that is strongly immunoreactive with the rabbit sera. Rabbit antibodies that react with the SjIR-12A fusion protein were immunoaffinity purified and used to localize immunoreactive product to the nervous tissue of male and female adult worms, the dorsal and lateral tegument of male adult worms, and in eggs to the miracidial tegument and the area between the eggshell and miracidium. Southern hybridization analysis suggests there are approximately four copies of the Sj70 gene per haploid genome.
Mol Biochem Parasitol 1987 Jul
PMID:Cloning of a Schistosoma japonicum gene encoding a major immunogen recognized by hyperinfected rabbits. 304 Dec 13


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