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A striking common O ‐linked N ‐acetylglucosaminyl moiety between cruzipain and myosin
Author(s) -
ACOSTA D. M.,
SOPRANO L. L.,
FERRERO M.,
LANDONI M.,
ESTEVA M. I.,
COUTO A. S.,
DUSCHAK V. G.
Publication year - 2011
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/j.1365-3024.2011.01291.x
Subject(s) - antigenicity , epitope , biology , myosin , polyclonal antibodies , antigen , immune system , microbiology and biotechnology , antibody , chagas disease , biochemistry , virology , immunology
Summary 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 O ‐GlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross‐reactivity between Cz 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 immune‐gold electron microscopy 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 Cz and either myosin or other cardiac O‐GlcNAc‐containing proteins, showing a new insight into the molecular immune pathogenesis of Chagas heart disease.