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 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

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

Protective immunity has been demonstrated in experimental schistosomiasis and is also believed to occur in man. It can be mediated by antibodies from infected animals or animals immunized with attenuated organisms. Recombinant Escherichia coli synthesizing antigenic polypeptides from the three principal species of schistosome that infect man, Schistosoma mansoni, S. japonicum and S. haematobium, have been constructed. Libraries of adult worm cDNA were prepared from each species in the expression vector lambda gt 11 and directly screened with antibodies from animals experimentally immunized with S. mansoni and S. japonicum and from humans infected with S. haematobium. The S. mansoni clones have been analysed in greatest detail. At least four different types of clones were identified. All the detected recombinant polypeptide antigens were recognised by antibodies from chronically infected mice and most were also recognised by antibodies from mice immunized with attenuated cercariae and anti-surface membrane antibodies. Clones synthesizing species-specific antigens for both S. mansoni and S. japonicum were identified by simultaneous screening of both libraries. At least three types of S. haematobium clones were identified by screening with human infection serum, most of which were species-specific. All the antigens were in the form of fusion peptides with E. coli beta-galactosidase and their expression was induced by isopropylthiogalactopyranoside. Since known protective monoclonal antibodies recognise highly glycosylated membrane proteins which cannot be identified in the form of nascent polypeptides, the direct identification of polypeptide antigens defined by their reactivity, as reported here, is an essential step in producing reagents by recombinant DNA technology, suitable for vaccination and diagnosis.
Mol Biochem Parasitol 1986 Feb
PMID:Adult schistosome cDNA libraries as a source of antigens for the study of experimental and human schistosomiasis. 293 4

The major cause of mortality in human schistosomiasis is the chronic granulomatous reaction of the liver tissue to Schistosoma mansoni eggs. Liver biopsy still provides the best evaluation of the degree of liver damage. However, liver biopsy does not provide an image of the dynamic process of fibrogenesis. Variations of concentrations of procollagen type III peptide in sera have been proposed to be significant markers of liver fibrosis. Thus, liver function tests in relation to histopathological diagnosis and procollagen type III peptide concentrations were studied in patients with schistosomiasis and revealed a high correlation between the serum procollagen type III peptide and the degree of fibrosis in liver tissue.
Exp Mol Pathol 1987 Jun
PMID:Serum concentration of N-terminal procollagen peptide of collagen type III in schistosomal liver fibrosis. 310 33

An expression plasmid pEx34b was used to synthesise parts of the 31/32 kDa Schistosoma mansoni antigens as fusions with the amino terminus of the phage MS2 polymerase. Purified MS2-schistosome fusion proteins reacted specifically in an enzyme-linked immunosorbent assay with sera from S. mansoni-infected patients. The observation that the majority of human sera tested recognised schistosome-specific epitopes, but not the MS2 polymerase fragment, suggests that the fusion proteins are useful for the immunodiagnosis of schistosomiasis and might be incorporated in a serological test system based on recombinant antigens.
Mol Biochem Parasitol 1988 Jan 15
PMID:Expression of diagnostic 31/32 kilodalton proteins of Schistosoma mansoni as fusions with bacteriophage MS2 polymerase. 312 31

Triton X-114 has been employed to isolate integral membrane proteins from Schistosoma japonicum and Schistosoma mansoni adult worms. Suitable marker molecules and antisera directed or raised against schistosome proteins partitioned by Triton X-114 extraction indicated that the phase separation and purification of integral membrane proteins had been successful and this fraction was free of contamination with aqueous (soluble) or secretory antigens. Two dimensional immunoblots further exemplified differences between antigens in the integral membrane protein extract and those of the aqueous fraction. Seven S. japonicum integral membrane proteins have been identified on immunoblots by serum from a hyperimmune and an infected rabbit and by sera from Philippine patients with a history of schistosomiasis japonica. Integral membrane proteins of S. mansoni and S. japonicum had surprisingly little conformity in the molecular weights and electrophoretic mobilities between the two species.
Mol Biochem Parasitol 1988 May
PMID:Immunoblotting analysis of the major integral membrane protein antigens of Schistosoma japonicum. 313 62

The effect of specific chemotherapy on hepatic fibrosis was studied in Swiss albino mice infected with Schistosoma mansoni. The effect of treatment with praziquantel at 8, 12, and 20 weeks postinfection on fibrosis was assessed by determination of total hepatic collagen content, ratio of type III/I + III collagen, granuloma volume, and histopathological examination of liver section. Total collagen content was reduced in mice treated at the 8th week of infection compared to respective infected controls. The ratio of type III/I collagen was within normal limits. The decrease in collagen deposition was not observed when treatment was given 12 or 20 weeks postinfection. Early specific treatment of schistosomiasis may be important in the therapeutic approach to the control of morbidity in schistosomiasis.
Exp Mol Pathol 1988 Oct
PMID:Effect of praziquantel on hepatic fibrosis in experimental Schistosomiasis mansoni. 313 42

The NH2-terminal amino acid sequence of the Mr 26 000 glutathione S-transferase (EC 2.5.1.18) of Schistosoma japonicum (Sj26) has been deduced by RNA and protein sequence analysis. Using this information, a bacterial plasmid has been constructed that directs the synthesis of the entire Sj26 molecule in Escherichia coli. Recombinant Sj26 exhibits glutathione S-transferase activity and can be readily purified from bacteria in a one-step procedure under non-denaturing conditions. The availability of recombinant Sj26 in essentially unlimited quantities will aid its assessment as a candidate vaccine molecule in schistosomiasis and could eventually lead to the rational design of a drug targetted on schistosome glutathione S-transferases.
Mol Biochem Parasitol 1988 Jan 15
PMID:Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase. 327 28


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