INVESTIGADORES
LANDONI Malena
artículos
Título:
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin.
Autor/es:
D.M. ACOSTA; L.L. SOPRANO; M. FERRERO; M. LANDONI; M. ESTEVA; A. S. COUTO,; V.G DUSCHAK,.
Revista:
PARASITE IMMUNOLOGY
Editorial:
WILEY-BLACKWELL PUBLISHING, INC
Referencias:
Lugar: Essex; Año: 2011
ISSN:
0141-9838
Resumen:
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.