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M Schechter

Publications and source records attributed to M Schechter.

At least 91 records · Page 5Linked to original sources
PubMed1986

Trypanosoma cruzi: characterization and isolation of a 57/51,000 m.w. surface glycoprotein (GP57/51) expressed by epimastigotes and bloodstream trypomastigotes.

We have recently described the application of a purified glycoprotein of 25,000 Mr (GP25) of Trypanosoma cruzi in serodiagnosis of Chagas' disease. Purified GP25 lacks appreciable immunogenicity in some animal species, in spite of being generally antigenic to parasitized hosts. The underlying cause for these contrasting observations has not been determined, but it may relate to the drastic extraction conditions used in the original isolation procedure, and possible damage inflicted to the native form of this antigen. This report describes the molecular properties of a GP25-related primary antigen, and a fast performance liquid chromatographic (FPLC) procedure to attain its isolation under gentle conditions. The expression of GP25-related antigen by epimastigotes or bloodstream forms was investigated with a high-affinity monoclonal antibody to GP25, SC11G10, as well as with monospecific antisera to GP25. Immunochemical analysis of Nonidet P-40 lysates supplemented with protease inhibitors indicated that GP25 is not synthesized as such; instead, a 57,000 Mr component (GP57) was identified as the primary antigen product. Partial enzymatic conversion to GP25 was observed when inhibitors were deliberately omitted from cell extracts. Most significantly, GP57 was established as the primary biosynthetic product in [35S]-labeled bloodstream trypomastigotes after immunoprecipitation with SC11G10 antibody. This analysis when applied to metabolically labeled epimastigotes has consistently revealed a minor antigen component of 51,000 Mr (GP51), in addition to GP57. The former was identified as the antigenically related product exposed at the parasite cell surface after external radioiodination of viable trypanosomes. Access to the native form of this widely distributed surface glycoprotein should stimulate the investigation of functional and structural aspects of its immunologic activity.

Animals↗
PubMed1986

Prevalence of antibodies to 72-kilodalton glycoprotein (GP72) in patients with Chagas' disease and further evidence of zymodeme-associated expression of GP72 carbohydrate epitopes.

Three competitive inhibition enzyme-linked immunosorbent assays were developed to examine the expression of the 72-kilodalton glycoprotein (GP72) and of a GP72 carbohydrate epitope in Trypanosoma cruzi strains and clones. A total of 148 strains and clones of known isozyme phenotype (principal zymodeme, Z) were tested. With monoclonal antibody 8G2B9 the enzyme-linked immunosorbent assay confirmed that the majority of Z1 strains and clones derived from them had undetectable levels of the carbohydrate epitope identified by antibody 8G2B9. This epitope was, however, readily detectable in all Z2, Z2(h), and Z3 strains and clones (P less than 0.001; 148 strains and clones tested). Zymodeme-associated differences in GP72 expression were not apparent from the enzyme-linked immunosorbent assay with monoclonal antibody WIC 226.4 (raised against periodate-treated GP72) or from that with rabbit anti-GP72 antiserum (84 or 119 strains and clones tested, respectively). Mice infected with culture-form metacyclic trypomastigotes of Z1, Z29, and Z3 or with blood-form trypomastigotes of Z1 and Z3 developed antibodies to affinity-purified GP72, showing that at least some GP72 epitopes are neither zymodeme specific nor stage specific. A total of 128 serum samples from patients with acute or clinically classified chronic Chagas' disease were assayed for immunoglobulin G (IgG) or IgM anti-GP72 antibodies. During the acute phase anti-GP72 IgM antibodies were elevated, whereas anti-GP72 IgG antibodies were low. There were no significant differences in anti-GP72 antibody levels among chronic-phase patient groups. Anti-GP72 antibodies were detected irrespective of the geographical origin of patients and irrespective of whether acute-phase blood parasitemias were due to Z1 (four patients) or Z2 (two patients).

Animals↗
PubMed1985

Further evaluation of lectin affinity purified glycoprotein (GP90) in the enzyme linked immunosorbent assay (ELISA) for diagnosis of Trypanosoma cruzi infection.

Sera from 143 patients considered to be infected with Trypanosoma cruzi on the basis of epidemiological, clinical and standard serological evidence gave positive results in the enzyme-linked immunosorbent assay (ELISA) using a lectin affinity purified 90,000 molecular weight glycoprotein (GP90) antigen preparation. Levels of antibody did not discriminate between clinically classified groups of patients in the chronic phase of infection. The GP90 preparation was found to be heterogeneous.

Adolescent↗
PubMed1985

Seniors in need.

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Aged↗
PubMed1984

Zymodeme and species specificities of monoclonal antibodies raised against Trypanosoma cruzi.

A series of hybrid cell lines was generated by the fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice that had been immunized or infected with Trypanosoma cruzi zymodemes (Z1, Z2, Z3 ). Four immunoglobulin isotypes, IgM, IgG1, IgG2a and IgG3 were represented amongst the monoclonal antibodies secreted by 22 hybridoma clones. On indirect immunofluorescence (IFAT) antibodies bound to flagellum, cytoplasm, cell membrane or stained the whole organism. Two antibodies were epimastigote-specific. Enzyme-linked immunosorbent assays (ELISA) and a dot immunobinding test were used to evaluate the zymodeme and species specificities of 13 antibodies: four reacted with all T. cruzi zymodemes tested, two reacted strongly with all except Z1, two predominantly with Z1, two predominantly with Z2, and three predominantly with Z3 . Two IgM antibodies cross reacted with Trypanosoma rangeli, T. brucei, Leishmania mexicana, L. braziliensis and L. donovani. Five antibodies were used in a preliminary immunobinding test, performed blindly, to compare monoclonal reactivities and zymodeme groups. The results suggested a correlation between the two methods of characterization. Anti-T. cruzi monoclonal antibodies are considered to have important applications to epidemiological studies and the improved diagnosis and prognosis of Chagas' disease.

Animals↗
PubMed1984

Speciality shops.

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Hospital Administration↗
PubMed1983

Purified Trypanosoma cruzi specific glycoprotein for discriminative serological diagnosis of South American trypanosomiasis (Chagas' disease).

Chagas' disease, leishmaniasis, and Trypanosoma rangeli infection are endemic and their distributions overlap in vast regions of South and Central America. Serological cross-reactivities can confuse epidemiological studies of these infections, and their differential diagnosis has been assigned a high priority by the World Health Organisation. A lectin-affinity-purified, 90,000 molecular weight glycoprotein (GP90) is present in the known principal strains (zymodemes) of Trypanosoma cruzi and absent from Leishmania and T rangeli. Patients with T cruzi infection have antibody to GP90, whereas patients with leishmaniasis do not and the two infections can be distinguished in an ELISA system using this antigen. In a mouse model, the same test can differentiate between T cruzi and T rangeli infections. Antigens purified by affinity chromatography clearly provide a practical basis for very precise, even strain-specific, diagnostic tests.

Antibodies↗