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Query: UNIPROT:P06889 (Mol)
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The isolation and characterization of a recombinant cDNA clone (OV7) expressing an antigen present in Onchocerca volvulus infective larvae and adult stages is described. Using chimpanzee antiserum generated against irradiated infective larvae, we isolated a cDNA clone from a lambda gt11 cDNA expression library derived from adult O. volvulus mRNA. The open reading frame encodes 131 amino acids corresponding to a 15.2-kDa protein. Affinity purified antibodies which bound specifically to OV7 fusion polypeptide recognized a single antigen with an apparent molecular weight of 17,000 in extracts of L3, L4 and adult worms. Immunoelectron microscopy established that the antigen encoded by this clone is present in the hypodermis and the basal layer of the cuticle of L3 and female adult worm, and in the egg shell around developing microfilariae. Since the OV7 fusion polypeptide is onchocerca-specific and is recognized specifically by sera from onchocerciasis patients, and sera from non-patent but infected chimpanzees, and not by sera from patients with other filarial parasites, it may have potential as an antigenic component in a test for detection of non-patent and patent infections of O. volvulus. The OV7 amino acid sequence contains residues that have a probable homology with the cysteine proteinase inhibitor superfamily.
Mol Biochem Parasitol 1991 Mar
PMID:Characterization of an Onchocerca volvulus cDNA clone encoding a genus specific antigen present in infective larvae and adult worms. 205 41

Recombinant cDNAs expressing an immunodominant antigen (Onchoag-1) of Onchocerca volvulus were identified by immunoscreening a cDNA expression library. The Onchoag-1 cDNAs are derived from an 8-kb mRNA that codes for a protein with an apparent molecular mass of 200 kDa. Indirect immunofluorescence using antisera against a recombinant fusion protein showed that Onchoag-1 is located in the muscle tissues of adult O. volvulus. The 2-kb sequence of one of the cDNAs contains a single open translation reading frame that encodes a protein with sequence similarities to Caenorhabditis elegans myosin heavy chain. Analysis of the 3' region of Onchoag-1 chromosomal gene reveals that it is frequently interrupted by short introns that follow the GT/AG rule at their splice sites. Studies on this myofibrillar antigen should contribute to our understanding of muscle function in O. volvulus as well as provide useful insight to the genesis of the immunopathological damage that is often associated with allergic reactions (the Mazzotti reactions) in onchocerciasis patients, following the administration of a chemotherapeutic agent such as diethylcarbamazine.
Mol Biochem Parasitol 1990 May
PMID:Characterization of a myosin-like antigen from Onchocerca volvulus. 219 23

A novel type of N-acetyltransferase, clearly different from the nuclear and cytosolic polyamine N-acetyltransferases of mammals, was recently found in the intestinal nematode Ascaris suum. The occurrence of this putrescine N-acetylating enzyme has also been noted in the filarial parasite Onchocerca volvulus. The enzyme was partially purified from adults of O. volvulus and A. suum by chromatography on DEAE-cellulose and cadaverine-Sepharose. Substrate specificities of the filarial enzyme resemble those of the N-acetyltransferase from A. suum, with respect to its preference for putrescine and other diamines above polyamines and histones. Additionally, both nematode enzymes acetylated histamine, whereas dopamine and serotonin were not accepted as substrates. The activities of the N-acetyltransferase from O. volvulus and A. suum were potently inhibited by the drug berenil; the type of inhibition was competitive with respect to putrescine. The inhibition constants for berenil were determined as 4.2 and 1.2 microM for the enzymes of O. volvulus and A. suum, the Km values for putrescine were found to be 330 microM and 250 microM, respectively. Putrescine N-acetyltransferase is discussed as a regulatory step in the degradation of excessive polyamines via polyamine oxidase to putrescine. At this branching point, putrescine is retained in the cell for de novo synthesis of spermidine and spermine, catabolized via diamine oxidase or acetylated to a suitable transport product for excretion.
Mol Biochem Parasitol 1990 Jan 01
PMID:Putrescine N-acetyltransferase in Onchocerca volvulus and Ascaris suum, an enzyme which is involved in polyamine degradation and release of N-acetylputrescine. 232 51

In order to analyse the developmental biology of Onchocerca spp. with a view to identifying molecules with specialised functions, we have devised a novel method for labelling proteins synthesised by larvae during growth in the vectors. Pulse labelling of Onchocerca lienalis by micro-injections of [35S]methionine into blackflies have revealed a major acidic protein of 23 kDa which is developmentally expressed almost exclusively by infective, third-stage larvae. The protein appears to be antigenically conserved between O. lienalis and Onchocerca volvulus, but exhibits size polymorphisms both among species and among individual organisms. It continues to be elaborated after terminal differentiation of the parasite in flies, but not by post-infective larvae entering the phase of development in the vertebrate host. A shift in temperature from 26 degrees C to 37 degrees C triggers secretion of the 23-kDa molecule as a discrete event 24-72 h after transmission. The labelling technique has been successfully employed with filarial species that develop in mosquitoes, and in principle should be widely applicable to the study of endoparasite gene expression within arthropods.
Mol Biochem Parasitol 1990 Mar
PMID:Developmentally regulated expression and secretion of a polymorphic antigen by Onchocerca infective-stage larvae. 232 57

The nucleotide sequence of a cDNA copy of the Dirofilaria immitis paramyosin gene was determined. The sequence was 2545 nucleotides in length, consisting of a single open reading frame of 848 amino acids capable of encoding a protein with a calculated molecular weight of 98,000. The cDNA clone was not complete, but probably includes over 97% of the coding region of the gene. We have previously observed that the cloned D. immitis paramyosin is recognized by sera from humans infected with Onchocerca volvulus. To determine the extent of homology at the protein level, we screened a cDNA library of O. volvulus with an antiserum made against D. immitis paramyosin. Ten recombinant clones were partially sequenced, comprising a total of 1186 nucleotides or 389 amino acids. The amino acid sequence of D. immitis paramyosin was 99% identical to the O. volvulus paramyosin. We also compared the amino acid sequence to other cloned paramyosins, and noted that 92% of the amino acids were identical to those of Caenorhabditis elegans, and 34% identical to those of Schistosoma mansoni. Comparison of the paramyosin sequence between different species revealed a hierarchy of similarities: (1) a 7-amino-acid repeat with apolar residues in the a and d position as the most conserved, followed by (2) the amino acid sequence and (3) the DNA sequence.
Mol Biochem Parasitol 1990 Jan 15
PMID:Filarial paramyosin: cDNA sequences from Dirofilaria immitis and Onchocerca volvulus. 232 8

We examined the ability of two filarial species, Onchocerca volvulus and Brugia malayi, to solubilize collagen molecules from native collagen fibrils. Collagenolytic activity was detected in extracts of adult worms, in living microfilariae of O. volvulus and in live infective larvae and adult female worms of B. malayi. Excretion-secretion factors produced in vitro by infective larvae of B. malayi also contained large amounts of collagenase. Studies with enzyme inhibitors suggest that the latter may be a metallo-protease. Antibodies to filarial collagenase were present in sera from patients with onchocerciasis and brugian filariasis and from mice immunized with B. malayi. These antibodies and a monoclonal antibody raised against O. volvulus antigens immunoprecipitate filarial collagenase but appear not to be directed against the active site of the enzyme.
Mol Biochem Parasitol 1986 Apr
PMID:Studies on a filarial antigen with collagenase activity. 242 72

Adults of Onchocerca volvulus and Onchocerca gibsoni were identically fractionated into a surface-enriched fraction, a phosphate buffered saline (PBS) extract and a PBS insoluble-detergent soluble fraction. Glycoproteins were prepared from these extracts and all fractions were examined by the Western blot technique using sera from individuals infected with a variety of filarial and non-filarial nematode worms. Using antisera to O. volvulus, a number of antigens were demonstrated in all of the extracts, with some antigens of each extract being unique. Many antigens were glycoproteins, and a high cross-reactivity was observed between O. volvulus and O. gibsoni. The different fractions of both species were also analysed using a panel of different sera in order to identify Onchocerca-specific antigens. The studies revealed that the lower molecular weight antigens showed greater Onchocerca specificity in all of the extracts examined. The surface-enriched fraction, however, clearly contained less widely cross-reacting components than the somatic and glycoprotein fractions. Finally, using surface labelling and coprecipitation techniques, O. gibsoni was shown to possess a 20 kDa Onchocerca-specific antigen, previously described for O. volvulus. The findings indicate a number of Onchocerca-specific antigens which may have potential in diagnosis of human onchocerciasis. They also show that the related bovine parasite O. gibsoni, may be an alternative source of material.
Mol Biochem Parasitol 1986 Sep
PMID:Identification of antigens of Onchocerca volvulus and Onchocerca gibsoni for diagnostic use. 242 80

Adult Onchocerca volvulus were isolated from nodules removed from onchocerciasis patients at four locations--two in the West African Sudan-savanna region (near Bamako, Mali, and Touboro, Cameroon), one in a West African forest region (Kumba, Cameroon) and one near Guatemala City, Guatemala. Four different cDNA expression libraries were constructed in bacteriophage lambda gt11 using poly(A)+ RNA from the adult female worms. Individual cDNA clones of single copy genes were used to compare the genomes of parasites from the different locales and to show that the haploid genome of O. volvulus is 1.5 x 10(8) base pairs. About 1 in 700 recombinant clones in each of the four amplified cDNA libraries produces a fusion protein recognized by pooled human anti-O. volvulus antisera. Partial sequence determination of a 2.0 kb cDNA clone for an O. volvulus protein that induces an immunodominant response in rabbits revealed that this antigen has sequence similarities with Caenorhabditis elegans myosin and with schistosome paramyosin (which confers partial protection against schistosome infection). The four cDNA libraries have been deposited with American Type Culture Collection (ATCC), 12301 Parklawn Drive, Rockville, MD 20852, U.S.A., for general distribution under ATCC Number 37509.
Mol Biochem Parasitol 1988 Dec
PMID:Construction of Onchocerca volvulus cDNA libraries and partial characterization of the cDNA for a major antigen. 246 64

The cDNA synthesized from mRNA of Dirofilaria immitis female adult worms was cloned into the expression vector lambda gt11. Screening the library with a hyperimmune rabbit antiserum raised against adult worm homogenates yielded several antigen positive clones. One of these clones, lambda cDi2, was recognized by rabbit antisera raised against either D. immitis L-3, adult, Brugia malayi L-3 or Onchocerca volvulus adult worm antigen, as well as by antisera from humans naturally infected with O. volvulus or Wuchereria bancrofti. Affinity-purified anti-lambda cDi2 antibodies reacted with a 97-kDa protein on Western transfers of adult D. immitis antigen extracts that were reduced with beta-mercaptoethanol. The whole rabbit anti-D. immitis adult antiserum depleted of anti-lambda cDi2 antibodies exhibited decreased reactivity to this 97-kDa band. A monoclonal antibody (IA6) that specifically binds Schistosoma mansoni paramyosin also recognised a 97-kDa protein in D. immitis extracts upon Western transfer. The deduced amino acid sequence of partial DNA sequence from lambda cDi2 showed some similarity to nematode myosin, and gave a stretch of 82 amino acids that is 91.5% identical to Caenorhabditis elegans paramyosin: thus, lambda cDi2 encodes D. immitis paramyosin.
Mol Biochem Parasitol 1989 Jun 01
PMID:A lambda gt11 cDNA recombinant that encodes Dirofilaria immitis paramyosin. 252 35

A genomic DNA library of a Liberian strain of Onchocerca volvulus was prepared in the vector bacteriophage lambda gt10. The library was differentially screened by hybridisation with radiolabelled total DNA from the homologous parasite, two heterologous Onchocerca parasites (Onchocerca gibsoni and Onchocerca gutturosa) and human liver cells. A clone (C1A1) was isolated whose binding to O. volvulus DNA was at least 50 times stronger than to the other parasite DNA samples. No binding was observed with human DNA. The insert of C1A1 was subcloned into the filamentous phage vector M13 mp18 and sequenced. Two oligonucleotides, each corresponding to a unique region of 60 nucleotides (out of a total of 154) were synthesised and examined for hybridisation with three different geographical isolates of O. volvulus (including forest and savannah strains) and six other Onchocerca spp. One of the oligonucleotides (C1A1-2) was found to hybridise to the three O. volvulus isolates with an intensity in the region of 300 times greater than to any other Onchocerca spp. Since the other species include the two which may be most closely related to O. volvulus, i.e., O. gibsoni and Onchocerca ochengi, it is concluded that C1A1-2 is likely to represent a truly species-specific probe.
Mol Biochem Parasitol 1989 Jun 15
PMID:An oligonucleotide probe specific for Onchocerca volvulus. 252 65


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