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)

We have characterized actin gene expression in Schistosoma mansoni at the RNA and protein levels. Northern blot analyses showed two size classes of actin mRNA in eggs, cercariae and adult worms of both sexes, approximately 1 900 and 1 400 bases in length. A higher abundance of actin mRNA of both size classes was demonstrated in male worms than in eggs, cercariae, and females. Using a phalloidin-rhodamine conjugate, male worms were observed to contain more actin protein than females. Southern blot-hybridization indicated that the sexual differences in actin mRNA and protein levels were not related to some S. mansoni actin genes being sex linked. In addition, two other trematodes, Schistosoma japonicum and Fasciola hepatica and a cestode, Taenia pisiformis contained two classes of actin mRNA similar in size as those in S. mansoni. In contrast, a turbellarian, Dugesia tigrina contained only a single short actin message size class approximately 1 400 bases in length.
Mol Biochem Parasitol 1985 Dec
PMID:Stage and sex specific differences in actin gene expression in Schistosoma mansoni. 241 16

We have cloned a gene encoding a 22.6 kDa antigen from a Schistosoma mansoni cDNA library. Northern blots indicate that transcription of this antigen occurs in adults and sporocysts but not in cercariae, eggs or in newly-transformed schistosomula. Immunoprecipitation and Western blotting with specific antisera indicate that the antigen is not detectable in the newly transformed schistosomulum but appears within 24 h of schistosomulum transformation. Indirect immunofluorescence of adult worms shows this protein to be located in the tegument.
Mol Biochem Parasitol 1986 Sep
PMID:Cloning of a developmentally regulated tegument antigen of Schistosoma mansoni. 242 81

An immunoradiometric assay has been used to determine the rate of loss of host erythrocyte antigen from the tegumental surface of adult Schistosoma mansoni. Host antigens were lost from the parasite surface with a half-time of up to 45 h during chase incubation in vitro, and with a half-time of about 5 days during residence in vivo in naive recipient hamsters. Since the host antigens were associated intimately with the outer bilayer of the tegument surface, it is suggested that the rate of surface turnover may similarly be very low. The implications of these findings for immune evasion by the adult parasite are discussed.
Mol Biochem Parasitol 1987 Sep
PMID:The outer bilayer of the adult schistosome tegument surface has a low turnover rate in vitro and in vivo. 244 82

A cDNA library derived from messenger RNA of adult Schistosoma mansoni was constructed in lambda gt11 and schistosome antigens were expressed as fusions with the amino terminus of the beta-galactosidase of Escherichia coli. Using mouse and human infection sera, recombinant clones specific for a 31/32 kDa doublet having a potential in the immunodiagnosis of schistosomiasis were selected. The specificity of the clones was verified by their reactivity with monoclonal antibodies. The identity of the cloned epitopes with those of the native proteins was confirmed by Western blot analysis of total schistosome proteins, using both antibodies affinity purified from the fusion proteins and antisera raised in rabbits against the fusions. The reactivity of the cloned antigens with human infection sera suggests their usefulness for the immunodiagnosis of human schistosomiasis.
Mol Biochem Parasitol 1987 Oct
PMID:Cloning of diagnostic 31/32 kilodalton antigens of Schistosoma mansoni. 244 97

The cercarial acetabular gland proteinase of Schistosomatium douthitti, an agent of 'swimmer's itch', has been identified and characterized. Like the corresponding proteinase of Schistosoma mansoni, it has significant elastase activity and can degrade a model of dermal extracellular matrix. However, unlike the S. mansoni enzyme, it has a higher molecular weight (50,000 versus 30,000), is of a different proteinase class (metallo versus serine), and has no significant primary structure homology to the S. mansoni proteinase. While these findings indicate that the failure of S. douthitti to produce chronic schistosomiasis in humans is not due to its lacking, or having a less potent 'penetration proteinase' than S. mansoni, the proteolytic enzymes are sufficiently different to support the hypothesis that the Schistosomatium line diverged quite early from the main branch of Schistosoma evolution.
Mol Biochem Parasitol 1988 Mar
PMID:The Schistosomatium douthitti cercarial elastase is biochemically and structurally distinct from that of Schistosoma mansoni. 245 79

Antigenic sites on the 31 kDa diagnostic protein of Schistosoma mansoni (Sm31) were identified using the cDNA fragment H3 cloned in the expression vector pEx34b. This fragment encodes approximately two-thirds of the polypeptide. A set of deletion mutants was generated by the exonuclease Bal31 and the resulting shortened proteins synthesised in Escherichia coli as fusions to MS2 polymerase were tested in Western blots with human schistosomiasis patient sera. Three antigenic regions were identified, one of which was narrowed down by appropriate restriction sites to a sequence specifying only 27 amino acid residues. Examination of a longer MS2 fusion product extending into the N-terminus of the protein, corresponding to the nearly full length Sm31 sequence, revealed that its reactivity in immunoblots is comparable with that of the H3 clone. This suggests that additional antigenic sites, which might be more reactive than those already identified, are absent from the remaining part of the protein.
Mol Biochem Parasitol 1988 Jul
PMID:Schistosoma mansoni: localisation of antigenic regions on the 31 kilodalton diagnostic protein. 245 63

Constitutively expressed schistosome homologues of heat-shock protein Hsp70 elicit a dominant antibody response in humans infected with either Schistosoma japonicum or Schistosoma mansoni; in each case the parasite antigens are immunologically distinct and noncrossreactive. The antigenic site of the homologues is located near their carboxyl terminus where phylogenetic divergence between Hsp70 proteins is greatest. Nucleotide sequence comparison between these regions predicts very few amino acid differences between the schistosome protein and that of their human host. Thus strikingly limited diversity is sufficient to elicit a discriminatory antibody response to these parasite host-like antigens.
Mol Biochem Parasitol 1988 Jun
PMID:Schistosome heat-shock proteins are immunologically distinct host-like antigens. 245 5

We have demonstrated previously in a mouse model that effective chemotherapy against Schistosoma mansoni with praziquantel (PZQ) is dependent upon an intact host antibody response. In the same study, it was found that worms recovered from PZQ-treated animals display surface-bound antibodies. In order to identify the target antigens of the antibodies involved in the synergy between PZQ and the immune response, monoclonal antibodies (mAbs) and polyclonal antisera recognizing different tegumental components were tested by indirect immunofluorescence (IF) assay for their ability to bind in vitro to the surface of 6-week-old schistosomes perfused from nude (athymic) mice 1 h after PZQ treatment. Nude mice were used as hosts because worms from these animals were found to lack bound anti-schistosome antibodies. Only 5 of the 21 antibodies tested reacted with drug-treated worms. This indicated that the damage caused by PZQ to the schistosome tegument is restricted to specific tegumental components. Of the positive reactions, one group of antibodies gave IF patterns different from, whereas the other group gave IF reactions similar to those seen with worms perfused from immunologically intact mice. Antibodies against a schistosome esterase and alkaline phosphatase produced reaction patterns in the former category. In contrast, two out of three monoclonal antibodies recognizing different epitopes on a 200-kDa glycoprotein abundant in worm tubercles gave IF patterns very similar to those observed on schistosomes from drug-treated, intact mice. The biological significance of these reactions was confirmed by demonstrating that transfer of one of the positive monoclonal antibodies to 6-week-infected, B cell-depleted (mu-suppressed) mice reconstitutes the efficacy of PZQ treatment to normal levels. The above results suggest that the antibodies involved in the mechanism of action of PZQ react with a limited set of antigens. Furthermore, they implicate the 200-kDa tubercle protein as a major target of this response in naturally infected hosts.
Mol Biochem Parasitol 1989 May 01
PMID:Role of host antibody in the chemotherapeutic action of praziquantel against Schistosoma mansoni: identification of target antigens. 249 7

We have characterized sulfated glycosaminoglycans of periovular granulomas induced in mouse liver by experimental infection with Schistosoma mansoni and determined parameters of their synthesis and accumulation by metabolic incorporation of 35S. The major component of glycosaminoglycans isolated from granulomas was dermatan sulfate and the minor component was heparan sulfate. A similar proportion was observed among newly synthesized 35S-labeled glycosaminoglycans, with a slight increase in the relative amount of heparan sulfate. Neither qualitative nor quantitative differences were observed between glycosaminoglycans isolated from granulomas of the acute and the chronic phase of the disease. In contrast, collagen content of granulomas increased eightfold during evolution of the disease from the acute to the chronic phase. It may be concluded that different mechanisms control glycosaminoglycan and collagen synthesis in schistosomal granulomas, as well as the ratio between these components in the extracellular matrix. This is consistent with the loose organization of the extracellular matrix in acute inflammatory reactions and its dense organization in the chronic reactions.
Exp Mol Pathol 1989 Jun
PMID:Patterns of sulfated glycosaminoglycan synthesis and accumulation in hepatic granulomas induced by schistosomal infection. 249 23

The activities of aspartate aminotransferase (AST) (EC.2.6.1.1.) I, alanine aminotransferase (ALT) (EC.2.6.1.2) II and lactate dehydrogenase (LD) (EC.1.1.1.27) III have been measured in tissue homogenate and in haemolymph of Biomphalaria alexandrina snails, the specific intermediate host for the human parasitic disease schistosomiasis due to Schistosoma mansoni.
Cell Mol Biol 1989
PMID:Selected enzymatic activities in fresh water snails, specific intermediate host for human schistosomiasis. 249 22


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