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Query: UNIPROT:P06889 (Mol)
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The human and animal filarial parasites Onchocerca volvulus, Dirofilaria immitis, Brugia patei and Litomosoides carinii contained low levels of putrescine but much higher levels of spermidine and spermine as estimated by ion-pair high pressure liquid chromatography; N-acetylated polyamines were present only in minute amounts. Enzyme activities of ornithine decarboxylase (EC 4.1.1.17) and arginine decarboxylase (EC 4.1.1.19), respectively, were not detectable. Experiments carried out with O. volvulus and D. immitis demonstrated the uptake and bioconversion of labeled polyamines. There is evidence for the existence of a complete reverse pathway generating putrescine from spermidine and spermine, respectively, in both worms. N-Acetylating enzyme activities were detected in 100,000 X g preparations of homogenates from D. immitis which were capable to acetylate putrescine, spermidine and spermine. Long term incubation of the worms in the presence of labeled polyamines resulted in the excretion of putrescine and N-acetylputrescine.
Mol Biochem Parasitol 1987 Jun
PMID:Polyamine metabolism in filarial worms. 362 68

Chemical analysis of adult females of Onchocerca gibsoni gave estimated chitin contents of 200-500 micrograms (g dry weight)-1. Egg shells from both O. gibsoni and Onchocerca volvulus stained with Calcofluor white and with fluorescent wheat germ agglutinin as shown by fluorescent light microscopy, and bound gold-labelled wheat germ agglutinin as shown by electron microscopy, under conditions specific for chitin. The egg shells appeared as single electron dense layers from 50 to 85 nm in thickness. Purified chitinase digested these egg shells, leaving coiled microfilariae unattacked. We conclude that chitin is a major component of the egg shells.
Mol Biochem Parasitol 1987 Oct
PMID:Chitin in egg shells of Onchocerca gibsoni and Onchocerca volvulus. 369 75

A technique employing Sephadex G25 gel filtration has been developed for the rapid isolation and purification of live microfilariae of Onchocerca volvulus from subcutaneous nodules and skin samples. Microfilariae, adult worms and L3 larvae have been surface radiolabelled using the Iodogen technique. Two proteins have been characterised on the surface of uterine microfilariae: these have apparent molecular weights of 14,800 and 15,000. A MW 15,000 protein was the only molecule labelled on the surface of skin microfilariae. Ten proteins were labelled on adult male worms: these have molecular weights of 15,000, 17,500, 20,000, 22,000, 24,000, 29,000, 32,000, 37,000, 42,000, and 50,000. Some, if not all, of these proteins were also identified on female worms. Seven proteins were labelled on the surface of L3 larvae: these have molecular weights of 17,500, 48,000, 50,000, 52,000, 54,000, 57,000, and 105,000. Three of the adult surface proteins were precipitated by selected human infection serum: these are the MW 17,500, 32,000 and 42,000 molecules. The microfilarial surface proteins were not precipitated by human infection serum. The antiserum used in these experiments was shown by Western blot analysis to contain high levels of antibody with specificity for microfilarial and adult antigens. Indirect immunofluorescent assays showed these sera to contain antibody which bound to the surface of adult worms and eggs but not microfilariae. The possibility that skin microfilariae absorb host serum albumin was investigated: Western blot analysis and surface immunofluorescence assays using a specific anti-human albumin serum gave negative results. Fluorescent lectin binding studies revealed the presence of stage-specific carbohydrate moieties exposed on the surface of adult worms and eggs. Microfilariae do not have surface carbohydrate determinants.
Mol Biochem Parasitol 1986 Mar
PMID:Surface components of Onchocerca volvulus. 396 55

NADP-linked malic enzyme (malate dehydrogenase (oxaloacetate-decarboxylating) NADP+, EC 1.1.1.40) has been partially purified from adult Onchocerca volvulus and Dirofilaria immitis. Suramin was found to inhibit the activity of malic enzyme from both filarial worms. The inhibition constants for suramin were calculated to be 0.011 microM and 0.015 microM for the enzymes from O. volvulus and D. immitis, respectively. In the case of NADP-linked malic enzyme from Trypanosoma brucei and chicken liver the inhibition by suramin was less pronounced. The inhibition constants were found to be 0.8 microM and 2.5 microM for the protozoan and vertebrate enzymes, respectively. The type of inhibition was competitive with respect to malate. The Michaelis constants for malate and pyruvate were determined to be 0.9 and 4.5 mM for O. volvulus and 0.85 and 5.0 mM for D. immitis, respectively. The low Km values for malate compared to those for pyruvate and the about 15-fold greater turnover in the direction of decarboxylation compared to carboxylation indicated that malic enzyme from both filarial sources might be involved in an alternative pathway leading from phosphoenolpyruvate via oxaleacetate, malate and pyruvate to lactate. It is suggested, that the inhibition of malic enzyme activity from O. volvulus by suramin might interfere with the generation of NADPH for biosynthetic reactions.
Mol Biochem Parasitol 1981 Nov
PMID:Inhibition of NADP-linked malic enzyme from Onchocerca volvulus and Dirofilaria immitis by suramin. 732 87

Polymerase chain reaction (PCR) products were characterized for a repeated sequence family (designated "O-150") of the human filarial parasite Onchocerca volvulus. In phylogenetic inferences, the O-150 sequences clustered into closely related groups, suggesting that concerted evolution maintains sequence homology in this family. Using a novel mathematical model based on a nested application of an analysis of variance, we demonstrated that African rainforest and savannah strain parasite populations are significantly different. In contrast, parasites collected in the New World are indistinguishable from African savannah strains of O. volvulus. This finding supports the hypothesis that onchocerciasis was recently introduced into the New World, possibly as a result of the slave trade.
Mol Biol Evol 1994 May
PMID:Recent evolutionary history of American Onchocerca volvulus, based on analysis of a tandemly repeated DNA sequence family. 751 98

Adaptive resonance theory (ART) describes a class of artificial neural network architectures that act as classification tools which self-organize, work in realtime, and require no retraining to classify novel sequences. We have adapted ART networks to provide support to scientists attempting to categorize tandem repeat DNA fragments from Onchocerca volvulus. In this approach, sequences of DNA fragments are presented to multiple ART-based networks which are linked together into two (or more) tiers; the first provides coarse sequence classification while the subsequent tiers refine the classifications as needed. The overall rating of the resulting classification of fragments is measured using statistical techniques based on those introduced by Zimmerman, et al. (1994) to validate results from traditional phylogenetic analysis. Tests of the Hierarchical ART-based Classification Network, or HABclass network, indicate its value as a fast, easy-to-use classification tool which adapts to new data without retraining on previously classified data.
Proc Int Conf Intell Syst Mol Biol 1994
PMID:DNA sequence analysis using hierarchical ART-based Classification Networks. 758 98

A recombinant lambda gt11 clone, IVGS3, encoding part of a 55-kDa antigen was isolated from an adult Schistosoma japonicum cDNA library. The protein expressed by this clone was recognised strongly by serum from rats that had been vaccinated with irradiated cercariae (VrS) rendering them highly immune to a challenge infection. Antibodies in VrS which were specific for IVGS3 did not recognise adult worm antigens of S. mansoni, suggesting that the recombinant antigen contains species-specific epitopes, although IVGS3 was weakly recognised by rat serum raised against irradiated S. mansoni cercariae, indicating the presence of a related antigen in this species. A further clone, AM1(p), was obtained which, together with IVGS3 encompasses the entire coding region of the gene which has been called Sj55. Sequence analysis revealed similarities with murine calreticulin, a protein resident in the endoplasmic reticulum. As with murine calreticulin, Sj55 was shown to be a calcium-binding protein. Antigens with homologies to calreticulin have also been described in two other helminths, S. mansoni and Onchocerca volvulus.
Mol Biochem Parasitol 1995 Apr
PMID:Cloning of a Schistosoma japonicum gene encoding an antigen with homology to calreticulin. 763 Mar 85

Several lines of evidence suggest that molting in parasitic nematodes is controlled through the action of steroid molting hormones, or ecdysones. In other organisms, the central mediator of steroid hormone action is the hormone receptor. These receptor molecules are members of a superfamily of proteins called the nuclear hormone receptor family. Using an oligonucleotide derived from the amino-acid sequence of the Drosophila melanogaster ecdysone receptor, genes encoding homologues of the nuclear hormone receptor family were identified in the genome of the human filarial parasite Onchocerca volvulus. The O. volvulus genome contains at least three genes that encode putative members of the nuclear hormone receptor superfamily. A complete cDNA for one of these genes, designated OvNHR-1, has been isolated and characterized. The OvNHR-1 cDNA was 2378 bp in length, and contained a single open reading frame of 1104 bp. The open reading frame encoded a peptide with all of the features characteristic of a member of the nuclear hormone receptor superfamily of proteins. OVNHR-1 appeared to be encoded by a single-copy gene. Expression of the mRNA corresponding to OvNHR-1 was developmentally regulated, with maximal expression occurring during early embryogenesis. The polypeptide encoded by the OvNHR-1 open reading frame is antigenic in a minority of individuals exposed to O. volvulus.
Mol Biochem Parasitol 1995 Mar
PMID:Characterization of genes encoding members of the nuclear hormone receptor superfamily from Onchocerca volvulus. 763 1

Little attention has been paid to the reproductive biology of filarial nematode parasites as a possible target for immunological or chemotherapeutic intervention. An interruption of the reproductive process would, in addition to breaking the cycle of transmission, reduce the morbidity associated with certain filarial infections. As part of our efforts to define molecules that have important functions during filarial embryogenesis, antibodies against embryo-associated proteins were used to identify a 6308-bp cDNA sequence (ovt1) from an Onchocerca volvulus cDNA expression library. The ovt1 cDNA contained an open reading frame that coded for 2022 amino acids. The deduced amino acid sequence was highly hydrophilic, alpha-helical in nature and included two leucine zipper domains. OVT1 also contained a single Arg-Gly-Asp (RGD) site. The results of Southern blot analyses demonstrated that an ovt1-like gene occurs in a number of different species of filarial nematodes. In situ hybridization experiments to identify tissues that contain ovt1 transcripts showed that ovt1 was transcribed at high levels in the late morula/early blastocyst stage of embryonic development. Transcripts for ovt1 were also detected in O. volvulus larvae and in the hypodermal cells of adult parasites. Two fragments of ovt1 were expressed as fusion proteins and the fusion proteins were used to produce antibodies in rabbits. Both antibodies recognized a native protein with an apparent molecular mass of 230 kDa in extracts from gravid female O. volvulus. In addition, the antibodies reacted with a restricted number of lower-molecular mass bands which may represent the products of post-transcriptional or post-translational processing. The predicted coiled-coil structure and the sites of transcription suggest that OVT1 may be a component of the extracellular matrix.
Mol Biochem Parasitol 1995 Feb
PMID:Molecular cloning of a gene expressed during early embryonic development in Onchocerca volvulus. 777 81

The full-length cDNA corresponding to an Onchocerca volvulus antigen, OvMBP/11, which had been selected as a serodiagnostic tool was isolated, sequenced, and the native antigen encoded by the cDNA characterised. The cDNA encodes a protein of 20.5 kDa (termed Ov 20) containing a putative signal peptide. Southern blot analysis indicates that there is only a single O. volvulus gene corresponding to Ov 20 but it has significant sequence similarity to genes corresponding to two 20.5-kDa predicted proteins of Caenorhabditis elegans. Homologues of the Ov 20 gene were detected at high stringency by Southern blot in the other Onchocerca species O. gibsoni, and O. gutturosa and at lower stringency in the related filarial nematodes Brugia malayi and Acanthocheilonema viteae. The Ov 20 native antigen has two molecular mass forms, 20 and 22 kDa, in all the life cycle stages studied. These isoforms have different levels of N-linked glycosylation on a peptide backbone of 17.5 kDa. Immunolocalisation and in situ hybridisation studies demonstrated that Ov 20 is transcribed and translated in the body wall of adult females and also in microfilariae, third and fourth stage larvae. Antigen was detected in the supernatant of in vitro cultured adult female nematodes. The B. malayi and A. viteae homologues are antigenically cross-reactive to Ov 20, share the same size peptide backbone but differ in their degree of glycosylation.
Mol Biochem Parasitol 1995 Feb
PMID:Characterisation of an immunodominant glycoprotein antigen of Onchocerca volvulus with homologues in other filarial nematodes and Caenorhabditis elegans. 777 83


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