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D Afchain

Publications and source records attributed to D Afchain.

At least 37 records · Page 2Linked to original sources
PubMed1984

Adjuvant requirements for protective immunization of mice using a Trypanosoma cruzi 90K cell surface glycoprotein.

A wide range of adjuvants including alhydrogel, saponin, Corynebacterium parvum, DDAB, Pfizer CP-20,961, oil adjuvants and several MDP analogues have been compared for their adjuvant activity in protecting mice against lethal Trypanosoma cruzi infection following immunization with a T. cruzi 90K cell surface glycoprotein. Only saponin was found to be effective. Promotion did not correlate with the ability to promote a particular Ig isotype; however, saponin was unique in its ability to promote cell-mediate immunity against the 90K glycoprotein.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1984

Different monoclonal antibodies against the component 5 specific for Trypanosoma cruzi.

Three murine monoclonal antibodies (I-35/67, II-190/30, III-160/18) produced by immunization against total epimastigote extract or component 5-enriched fractions of Trypanosoma cruzi (Tehuantepec strain) have been demonstrated to recognize the component 5 specific for T. cruzi. By immunofluorescence studies, one of these monoclonal antibodies (I-35/67) was shown to bind to the epimastigote cell surface, and the two others (II-190/30 III-160/18) were preferentially directed against internal subcellular organelles. Immunoprecipitation using these monoclonal antibodies followed by SDS-PAGE analysis, has led to identification of four molecules with apparent molecular weights of 72 Kd, 51 Kd, 43 Kd, and 24 Kd in T. cruzi epimastigotes. Potential uses of these monoclonal antibodies in serological tests and immunochemical analysis of target antigens are discussed.

Animals↗
PubMed1983

Parasitological and immunological aspects of Trypanosoma cruzi infection in nude rats.

The role of the thymus on immunity of rats against Trypanosoma cruzi infection was investigated in vivo. The athymic (nu/nu) rats were shown to be significantly more susceptible to the acute phase of the infection than the control nu/+ rats, as measured by increased parasitemia and mortality. Specific anti-T. cruzi antibodies, complement, IgM and IgG2a serum levels were determined. The results would indicate the essential role of antibodies in immunity to acute Chagas' disease through T-dependent immune response.

Animals↗
PubMed1983

Trypanosoma cruzi: variation in susceptibility of inbred strains of rats.

Eight strains of male rats (AUG, BN, LEW, LIS, WAG, F 344, LOU/M, DA) and 3 strains of female rats (LEW, F 344, KGH) were challenged with 15 X 10(4) trypomastigotes of the Tehuantepec strain of T. cruzi. Parasitemia and mortality were observed for 60 days. Varying degrees of susceptibility were demonstrated between strains: complete resistance (R), no parasitemia; low resistance (LR), mild parasitemia; and no resistance (NR), high parasitemia. The differences in susceptibility to T. cruzi, using inbred strains of rats, were unrelated to Rt-1 haplotype. However, the level of parasitemia and host survival are not necessarily related; both male and female F 344 hosts are susceptible (NR) to T. cruzi but only females survive.

Animals↗
PubMed1982

[Production of monoclonal antibody anti-antigen 5 for Trypanosoma cruzi].

Monoclonal antibodies against Trypanosoma cruzi have been produced by fusion of Sp 2/0 myeloma cells and splenic lymphocytes from BALB/c Mice immunized with a T. cruzi antigenic fraction. Antigenic studies of these monoclonal antibodies have led to the identification of IgG 1 antibody against the component 5 specific for T. cruzi (cellular clone II 190/151). These monoclonal antibodies will give rise not only to new diagnostic and epidemiological perspectives but will also aid in achieving a better understanding of the biological role of this antigen.

Animals↗
PubMed1982

Peanut agglutinin affinity chromatography of Trypanosoma cruzi glycoproteins.

Glycoproteins from Trypanosoma cruzi epimastigotes have been extracted by diiodosalycilic acid and lithium salts, and phenol-water biphasic partition. Peanut agglutinin has been used in a one step preparative method for fractionating the total extract in order to separate the so-called galactose-terminal glycoproteins. The different fractions have been studied by SDS electrophoresis, ultracentrifugation and immunoelectrophoresis techniques. The experimental immunogenicity, antigenicity and specificity of the PNA affinity fractions has been evaluated.

Animals↗
PubMed1981

Trypanosoma cruzi infection in B-cell-deficient rats.

The effect of neonatally initiated injections of anti-mu rabbit antiserum on immunity of rats against Trypanosoma cruzi infection was investigated in vivo. Anti-mu treatment resulted in a loss of immunoglobulin M (IgM) and IgG2a synthesis and, subsequently, of antibody production. These rats so treated were shown to be significantly more susceptible to the acute phase of the infection than the control rats treated with normal rabbit serum, as measured by increased parasitemia and mortality. These results indicate the essential role of antibodies, probably in association with complement or effector cells or both, in immunity to acute Chagas' disease.

Animals↗
PubMed1980

Circulating immune complexes and anti-IgG antibodies in mucocutaneous leishmaniasis.

Circulating immune complexes (CIC), anti-IgG, anti-DNA, and anti-collagen autoantibodies (Ab) were investigated in sera from patients with South American leishmaniasis. No significant levels of anti-DNA or anti-collagen autoantibodies were observed. Only a few patients with cutaneous leishmaniasis or with only one mucocutaneous lesion showed values for CIC and anti-IgG Ab higher than those in the control group. In contrast, both CIC and anti-IgG Ab were demonstrated in most patients with several lesions due to mucocutaneous leishmaniasis (MMC). Moreover, a close correlation was noticed between the detection of CIC and anti-IgG Ab in MMC patients. This relationship suggested that part of the detected CIC could have been formed by IgG-anti-IgG complexes. The involvement of these immunopathologically active substances in the clinical evolution of mucocutaneous leishmaniasis is discussed.

Antigen-Antibody Complex↗
PubMed1979

Antigenic make-up of Trypanosoma cruzi culture forms: identification of a specific component.

A comparison of Trypanosoma cruzi water soluble antigens with those of stercorarian and salivarian trypanosomes, and Leishmania using immunoprecipitation in gels and immunoelectrophoresis, with the aid of hyperimmune rabbit serum and heterologous adsorptions showed the following. 1) There is a high complexity of soluble antigens of T. cruzi and T. rangeli. 2) At the intraspecific level our results demonstrated the antigenic stability of T. cruzi when maintained in vitro, and that there was quantitative antigenic consistency of the culture forms of different strains of T. cruzi from diverse geographic and parasite sources. At the interspecific level, the antigenic relationships between T. cruzi and the other Trypanosomatidae were established, as follows: 6/10ths of the antigens are shared by stercorarian species (T. dionisii, T. rangeli); 4/10ths by a salivarian trypanosome (T. brucei); and 3/10ths by Leishmania (L. donovani, L. mexicana). 3) Among the 4/10ths of antigenic components specific to T. cruzi, one component was characterized by its antigenicity and immunogenicity in natural and experimental infections, and in immunization experiments; this component was specific to T. cruzi when compared to the other Trypanosomatidae antigens.

Animals↗
PubMed1978

Purification of a specific antigen of Trypanosoma cruzi from culture forms.

A monospecific rabbit antiserum was prepared against a specific component of Tryanosoma cruzi epimastigote culture forms (designated antigen 5). Rabbits were immunized intradermally in 30-50 sites with the zone of agarose gel in which the component 5:anti-5 complex was visualized after two-dimensional immunoelectrophoresis. With this appropriate antiserum and the total epimastigote soluble extracts, the specific component of T. cruzi was purified by immunoadsorption. Purity and specificity controls of thefinal product were carried out by prolonged immunization of rabbits, and then by immunoelectrophoretic and two-dimensional electrophoretic analyses.

Adsorption↗