A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin.

D.M. ACOSTA; L.L. SOPRANO; M. FERRERO; M. LANDONI; M. ESTEVA; A. S. COUTO,; V.G DUSCHAK,.

PARASITE IMMUNOLOGY

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Essex; Año: 2011

0141-9838

Single units of O-linked N-acetylglucosamine (GlcNAc), usually components of nuclear and cytoplasmatic proteins, are present at the C-Terminal domain of cruzipain (Cz), a lysosomal major antigen from Trypanosoma cruzi. On the other hand, antibodies directed against some self-antigens like myosin are associated with Chagas heart disease. The participation of OGlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between cruzipain and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immunogold electronmicroscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption, provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between cruzipain and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immunopathogenesis of Chagas heart disease. self-antigens like myosin are associated with Chagas heart disease. The participation of OGlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between cruzipain and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immunogold electronmicroscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption, provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between cruzipain and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immunopathogenesis of Chagas heart disease. self-antigens like myosin are associated with Chagas heart disease. The participation of OGlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between cruzipain and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immunogold electronmicroscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption, provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between cruzipain and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immunopathogenesis of Chagas heart disease. Trypanosoma cruzi. On the other hand, antibodies directed against some self-antigens like myosin are associated with Chagas heart disease. The participation of OGlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between cruzipain and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immunogold electronmicroscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption, provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between cruzipain and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immunopathogenesis of Chagas heart disease.