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)

Both the liver fluke Fasciola hepatica and the blood fluke Schistosoma mansoni have GTP-binding proteins which are part of the trans-membrane signalling system. These proteins require GTP in order to interact with the catalytic subunit of adenylate cyclase. The technique of immunoblotting was used in order to distinguish the GTP-binding proteins Gs, Gi, and Go. Immunoblotting was carried out using antisera prepared against peptides deduced from bovine cDNA clones specific for alpha or beta subunits of known G proteins. A 41-kDa Gs alpha has been identified in S. mansoni and a 42.5-kDa Gs alpha in F. hepatica. A 41-kDa Go alpha was found in both parasites. A 36-kDa G beta was identified in both parasites using antiserum made against bovine transducin.
Mol Biochem Parasitol 1989 Aug
PMID:Identification of GTP-binding proteins in Fasciola hepatica and Schistosoma mansoni by immunoblotting. 250 6

We report the sequence of a cDNA clone encoding an 86-kDa polypeptide antigen (p86) from Schistosoma mansoni. Fusion proteins made in Escherichia coli are recognized by human infection sera. The reading frame of this antigen is highly homologous to those of the large heat-shock proteins of Saccharomyces cerevisiae (HSP90) and Drosophila melanogaster (HSP83). mRNA encoding p86 increases in response to heat shock of adult worms, as does HSP70. Comparisons of the sequences of HSP70 and HSP83 homologues show that these two families of heat-shock proteins are not significantly related except for the last four amino acid residues, which are Glu-Glu-Val-Asp in every case. This sequence is not found at the carboxy terminus of any other protein in the current databases.
Mol Biochem Parasitol 1989 Aug
PMID:The 86-kilodalton antigen from Schistosoma mansoni is a heat-shock protein homologous to yeast HSP-90. 250 7

Total lipids were isolated from native and irradiated Biomphalaria alexandrina snails, specific intermediate hosts for Schistosoma mansoni.
Cell Mol Biol 1989
PMID:Studies on fresh water snails, specific intermediate hosts for schistosomiasis 1--isolation of total lipids from native and irradiated snails. 251 98

A DNA clone representing a 0.4 kb degenerative repeat has been isolated. The DNA sequence is present only in the genome of female Schistosoma mansoni at different stages of the life cycle, at a frequency of approximately 75 copies per adult female genome. The sequence is not expressed and probably represents satellite DNA in the heterochromatin region of the W chromosome. It is demonstrated that the DNA clone may be used for the rapid determination of the sex of cercariae without the need for DNA isolation or Southern blotting.
Mol Biochem Parasitol 1989 Feb
PMID:A DNA probe from Schistosoma mansoni allows rapid determination of the sex of larval parasites. 252 16

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

Recognition sites for nine different restriction endonucleases were mapped on rDNA genes of fasciolid species. Southern blots of digested DNA from individual worms were probed sequentially with three different probes derived from rDNA of Schistosoma mansoni and known to span between them the entire rDNA repeat unit in that species. Eighteen recognition sites were mapped for Fasciola hepatica, and seventeen for Fasciola gigantica and Fascioloides magna. Each fasciolid species had no more than two unique recognition sites, the remainder being common to one or both of the other two species. No intraspecific variation in restriction sites was noted in F. hepatica (individuals from 11 samples studied; hosts were sheep, cattle and laboratory animals; geographical origins. Australia, New Zealand, Mexico, U.K., Hungary and Spain), or in F. gigantica (two samples; Indonesia and Malaysia). Only one sample of F. magna was available. One specimen of Fasciola sp. from Japan (specific identity regarded in the literature as uncertain) yielded a restriction map identical to that of F. gigantica. Almost all recognition sites occurred in or near the putative rRNA coding regions. The non-transcribed spacer region had few or no cut sites despite the fact that this region is up to about one half of the entire repeat unit in length. Length heterogeneity was noted in the non-transcribed spacer, even within individual worms.
Mol Biochem Parasitol 1989 Oct
PMID:Restriction enzyme mapping of ribosomal DNA can distinguish between fasciolid (liver fluke) species. 255 11

Ribosomal gene probes were used to investigate the genetic basis of drug resistance in schistosomes in a model where resistance to the anthelmintic hycanthone (HC) is generated by exposing immature worms to the drug. Two strains of Schistosoma mansoni, JHU and NMRI, were used. Drug resistance could be produced in the JHU strain by treatment with HC, but was also found to occur spontaneously. In contrast, it was not possible to detect or produce resistance to HC in the NMRI strain. A genomic alteration accompanied the development of resistance. The change was evidence by the occurrence of restriction fragment length polymorphisms (RFLPs) when Southern blots of genomic DNA from HC-resistant worms were hybridized with the ribosomal probe pSM389, which contains part of the small rRNA gene plus non-transcribed spacer (NTS) sequence. The most reliable marker of HC-resistance was a 3.6-kb BamHI fragment which was present and heritable in 7 drug-resistant lines derived from the JHU strain but absent from the parent JHU population and from NMRI parasites. The universal absence of the 3.6-kb RFLP in HC-sensitive individuals and its presence in the drug-resistant progeny suggest that resistance results from an induced change in the population rather than from selection of HC-resistant parasites. The rRNA gene sequence responsible for detecting the 3.6-kb RFLP appears to be localized either to the NTS or to the 5' end of the small rRNA gene, since hybridization to a probe containing sequence from the rRNA gene contiguous and downstream from the insert of pSM389 failed to reveal the RFLP. These results show that the development of resistance to HC is accompanied by a genomic rearrangement.
Mol Biochem Parasitol 1989 Oct
PMID:A genomic change associated with the development of resistance to hycanthone in Schistosoma mansoni. 257 29

We have constructed cDNA clones containing the complete nucleotide sequences coding for two highly antigenic Schistosoma mansoni adult worm proteins, Sm31 and Sm32. The predicted amino acid sequence of Sm31 shows significant homology to mouse, rat and human cathepsin B. The nucleotide sequence of Sm32 is identical to that reported by others for S. mansoni "haemoglobinase'. The different nucleotide sequences demonstrate the existence of two different proteolytic enzymes, both of which are synthesised in the form of precursor molecules. Structural homology of the schistosome cathepsin B to the mammalian ones indicates that the mature protein is processed from a propeptide. The calculated molecular weight of haemoglobinase of 47,000 suggests that post-translational processing is also involved in generating an active protease.
Mol Biochem Parasitol 1989 Mar 01
PMID:Primary structures of Sm31/32 diagnostic proteins of Schistosoma mansoni and their identification as proteases. 272 81

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

A 476 bp fragment of female-specific Schistosoma mansoni genomic DNA, clone W1, represents a degenerative repeat present in more than 500 copies per female genome, and may be part of the constitutive heterochromatin of the W chromosome. The cloning method described can be used as a general approach for isolating sex-specific, repeated DNA fragments. Using W1 as a probe, we have developed a rapid and accurate dot-blot assay for determining the sex of S. mansoni cercariae.
Mol Biochem Parasitol 1989 Oct
PMID:Isolation of a female-specific, highly repeated Schistosoma mansoni DNA probe and its use in an assay of cercarial sex. 279 60


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