A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
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...
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todo:paper_01419838_v33_n7_p363_Acosta2023-10-03T14:58:50Z A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin Acosta, D.M. Soprano, L.L. Ferrero, M. Landoni, M. Esteva, M.I. Couto, A.S. Duschak, V.G. Chagas disease Cruzipain Myosin O-N-acetyl-d-glucosamine Trypanosoma cruzi aprotinin cruzipain epitope myosin n acetylglucosamine animal tissue article carboxy terminal sequence Chagas disease cross reaction enzyme linked immunosorbent assay heart immunogold electron microscopy mitochondrion mouse nonhuman pathogenesis priority journal Trypanosoma cruzi Acetylglucosamine Animals Antibodies, Protozoan Cross Reactions Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitopes Humans Mice Mice, Inbred BALB C Microscopy, Immunoelectron Myocardium Myosins Rabbits Trypanosoma cruzi Mus Oryctolagus cuniculus Trypanosoma cruzi 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. © 2011 Blackwell Publishing Ltd. Fil:Landoni, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Couto, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01419838_v33_n7_p363_Acosta |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Chagas disease Cruzipain Myosin O-N-acetyl-d-glucosamine Trypanosoma cruzi aprotinin cruzipain epitope myosin n acetylglucosamine animal tissue article carboxy terminal sequence Chagas disease cross reaction enzyme linked immunosorbent assay heart immunogold electron microscopy mitochondrion mouse nonhuman pathogenesis priority journal Trypanosoma cruzi Acetylglucosamine Animals Antibodies, Protozoan Cross Reactions Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitopes Humans Mice Mice, Inbred BALB C Microscopy, Immunoelectron Myocardium Myosins Rabbits Trypanosoma cruzi Mus Oryctolagus cuniculus Trypanosoma cruzi |
| spellingShingle |
Chagas disease Cruzipain Myosin O-N-acetyl-d-glucosamine Trypanosoma cruzi aprotinin cruzipain epitope myosin n acetylglucosamine animal tissue article carboxy terminal sequence Chagas disease cross reaction enzyme linked immunosorbent assay heart immunogold electron microscopy mitochondrion mouse nonhuman pathogenesis priority journal Trypanosoma cruzi Acetylglucosamine Animals Antibodies, Protozoan Cross Reactions Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitopes Humans Mice Mice, Inbred BALB C Microscopy, Immunoelectron Myocardium Myosins Rabbits Trypanosoma cruzi Mus Oryctolagus cuniculus Trypanosoma cruzi Acosta, D.M. Soprano, L.L. Ferrero, M. Landoni, M. Esteva, M.I. Couto, A.S. Duschak, V.G. A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| topic_facet |
Chagas disease Cruzipain Myosin O-N-acetyl-d-glucosamine Trypanosoma cruzi aprotinin cruzipain epitope myosin n acetylglucosamine animal tissue article carboxy terminal sequence Chagas disease cross reaction enzyme linked immunosorbent assay heart immunogold electron microscopy mitochondrion mouse nonhuman pathogenesis priority journal Trypanosoma cruzi Acetylglucosamine Animals Antibodies, Protozoan Cross Reactions Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitopes Humans Mice Mice, Inbred BALB C Microscopy, Immunoelectron Myocardium Myosins Rabbits Trypanosoma cruzi Mus Oryctolagus cuniculus Trypanosoma cruzi |
| description |
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. © 2011 Blackwell Publishing Ltd. |
| format |
JOUR |
| author |
Acosta, D.M. Soprano, L.L. Ferrero, M. Landoni, M. Esteva, M.I. Couto, A.S. Duschak, V.G. |
| author_facet |
Acosta, D.M. Soprano, L.L. Ferrero, M. Landoni, M. Esteva, M.I. Couto, A.S. Duschak, V.G. |
| author_sort |
Acosta, D.M. |
| title |
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| title_short |
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| title_full |
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| title_fullStr |
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| title_full_unstemmed |
A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin |
| title_sort |
striking common o-linked n-acetylglucosaminyl moiety between cruzipain and myosin |
| url |
http://hdl.handle.net/20.500.12110/paper_01419838_v33_n7_p363_Acosta |
| work_keys_str_mv |
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