Different Monoclonal Antibodies against the Component 5 Specific for Trypanosoma cruzi *

Orozco, Óscar; Afchain, D.; Dissous, Colette; Rodriguez, C.; Ovlaque, G; Lemesre, Jean-Loup; Loyens, Marc; Capron, Arnaud

doi:10.4269/ajtmh.1984.33.560

Cited by 19 publications

(9 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Most described here are IgM and only two of tbem are IgG. This high proportion of anti-T. crttzi IgM antibodies has been reported by other investigators (Orozco et at., 1984;Chao & Dusanie, 1985; Giovanni-De-Simone c/«/.. 1987). IgGl monoclonal antibodies (I63B6 and I63C3) recognize antigens ihat would bave an intracytoplasmic distribution, as suggested by the images obtained by IIF of formalin-treated epimastigotes fixed by heating.…”

Section: Discussionsupporting

confidence: 85%

Isolation of a Trypanosoma cruzi antigen by affinity chromatography with a monoclonal antibody. Preliminary evaluation of its possible applications in serological tests

Malchiodi

Chiaramonte

Isola

et al. 1990

Clinical and Experimental Immunology

View full text Add to dashboard Cite

By affinity chromatography with a monoclonal antibody (163B6), obtained in our laboratory, we have isolated a T. cruzi antigen which could be useful for differential diagnosis of Chagas' disease from leishmaniasis. This antigen, a 52-kD protein, reacted with all sera from Chagas' disease patients tested but not with sera from patients with leishmania, in ELISA. The 52-kD antigen is widely distributed in the Trypanosoma genus since the 163B6 monoclonal antibody reacts with T. rangeli and 8 strains and a clone of T. cruzi epimastigotes.

show abstract

Section: Discussionsupporting

confidence: 85%

Isolation of a Trypanosoma cruzi antigen by affinity chromatography with a monoclonal antibody. Preliminary evaluation of its possible applications in serological tests

Malchiodi

Chiaramonte

Isola

et al. 1990

Clinical and Experimental Immunology

View full text Add to dashboard Cite

show abstract

“…Ascitic fluids were produced in pristane-primed Balb/C mice and the mAb (clones Tg56/IgG 1 and Tg54/IgG2b) were purified by a 50% ammonium sulphate precipitation followed by a chromatography on DEAE-Trisacryl (IBF, Villeneuve la Garenne, France). Purified mAb against T. cruzi (Orozco et al 1984) was used as control.…”

Section: Anti-p30 Monoclonal Antibodiesmentioning

confidence: 99%

The immunodominant epitope of the major membrane tachyzoite protein (P30) of Toxoplasma gondii

Santoro

Charif

Càpron

1986

Parasite Immunology

Self Cite

View full text Add to dashboard Cite

Several physicochemical characteristics of the repeated epitope of the major surface protein (P30) of Toxoplasma gondii were investigated with an anti-P30 mAb by two different methods: a one-site/inhibition assay that detects molecules containing single or multiple epitopes and a two-site/one antibody radiometric assay that is only effective with antigenic molecules containing two or more identical epitopes. Using both techniques, the repeated epitope within purified P30 was stable after 1 h at 63 degrees C, but labile at 100 degrees C. It was also resistant to successive freezing and thawing, and not affected after one year at -70 degrees C. Lyophilization and acidic or basic treatment had no effect. This epitope was also resistant to 20% trichloroacetic acid precipitation (activity recovered in the pellet) and to precipitation with cold acetone. To investigate the immunodominance of this repeated epitope during the humoral immune response against T. gondii, competition binding assays between anti-P30 mAb and polyclonal antibodies, from rabbits immunized with either purified P30 or total Toxoplasma extract and from patients with toxoplasmosis, have been used. We found that the mAb inhibited 50-95% of the binding of the IgG antibodies from both rabbits to purified P30. In addition, the binding of both human IgG and IgM antibodies to P30 was significantly inhibited by the mAb. It appears, therefore, that a single region of P30 contains most of the immunogenic activity.

show abstract

“…In this study, 25-50% of the binding of the different human IgG antibodies to the solid phase-associated Toxoplasma antigen was inhibited by each of the mAb directed to p30. An excess of the unrelated mAb anti-T. cruzi [14] had no inhibitory effect. It appears, therefore, that in the patients with a recent or past Figure 2.…”

Section: Resultsmentioning

confidence: 88%

Major surface protein of Toxoplasma gondii (p30) contains an immunodominant region with repetitive epitopes

et al. 1985

View full text Add to dashboard Cite

Four monoclonal antibodies (mAb) against surface antigens of tachyzoites of Toxoplasma gondii were produced. Immunoprecipitation of extracts of 125I-labeled tachyzoites identified the same polypeptide with apparent molecular weight of 30 000 (p30). A competition binding assay indicated that a single region of p30 was recognized by all 4 of the mAb. Furthermore, we found that single mAb inhibited 25-50% of the specific binding of antibodies of patients with toxoplasmosis to the antigenic extract of tachyzoites. It appears, therefore, that p30 is the most immunogenic constituent of tachyzoites, and that a single region of this molecule contains most of the immunogenic activity. Finally, a two-site/one-antibody immunoradiometric assay with the same mAb indicated that the p30 molecule is multivalent with respect to the expression of a single epitope.

show abstract

Different Monoclonal Antibodies against the Component 5 Specific for Trypanosoma cruzi *

Cited by 19 publications

References 0 publications

Isolation of a Trypanosoma cruzi antigen by affinity chromatography with a monoclonal antibody. Preliminary evaluation of its possible applications in serological tests

Isolation of a Trypanosoma cruzi antigen by affinity chromatography with a monoclonal antibody. Preliminary evaluation of its possible applications in serological tests

The immunodominant epitope of the major membrane tachyzoite protein (P30) of Toxoplasma gondii

Major surface protein of Toxoplasma gondii (p30) contains an immunodominant region with repetitive epitopes

Contact Info

Product

Resources

About