Artículo

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" (2011) Parasite Immunology. 33(7):363-370
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Abstract:

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.

Registro:

Documento: Artículo
Título:A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
Autor:Acosta, D.M.; Soprano, L.L.; Ferrero, M.; Landoni, M.; Esteva, M.I.; Couto, A.S.; Duschak, V.G.
Filiación:Instituto Nacional de Parasitología Dr Mario Fatala Chaben, ANLIS-Malbrán, Ministerio de Salud de la Nación, Buenos Aires, Argentina
CIHIDECAR (CONICET) Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave: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
Año:2011
Volumen:33
Número:7
Página de inicio:363
Página de fin:370
DOI: http://dx.doi.org/10.1111/j.1365-3024.2011.01291.x
Título revista:Parasite Immunology
Título revista abreviado:Parasite Immunol.
ISSN:01419838
CODEN:PAIMD
CAS:aprotinin, 11004-21-0, 12407-79-3, 50936-63-5, 52229-70-6, 58591-29-0, 9050-74-2, 9075-10-9, 9087-70-1; n acetylglucosamine, 7512-17-6; Acetylglucosamine, 7512-17-6; Antibodies, Protozoan; Cysteine Endopeptidases, 3.4.22.-; Epitopes; Myosins, 3.6.4.1; cruzipain, 3.4.22.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01419838_v33_n7_p363_Acosta

Referencias:

  • , p. 425. , Estimación cuantitativa de la Enfermedad de Chagas en las Américas Organización Panamericana (OPS) de la Salud. Ref type Pamphlet. Geneva, Pan American Health Organization/World Health Organization, 525 23rd Street, NW Washington, DC 20037, USA. Department of Control of Neglected Tropical Diseases (NTD). OPS/HDM/CD/-2006;; Schmunis, G.A., Epidemiology of Chagas disease in non-endemic countries: the role of international migration (2007) Mem Inst Oswaldo Cruz., 102 (SUPPL. I), pp. 75-85
  • Gascon, J., Bern, C., Pinazo, M.J., Chagas disease in Spain, the United States and other non-endemic countries (2010) Acta Trop, 115, pp. 22-27
  • (1984) Panamerican Health Organization Status of Chagas Disease in the Region of Americas. Epidemiologic Bulletin, , Pan American Health Organization. Washington, DC, Pan American Health Organization
  • Leon, J.S., Engman, D.M., The significance of autoimmunity in the pathogenesis of Chagas heart disease (2003) Front Biosci, 8, pp. 315-322
  • Tarleton, R.L., Parasite persistence in the etiology of Chagas disease (2001) Int J Parasitol, 31, pp. 550-554
  • Duschak, V.G., Couto, A.S., Cruzipain, the major cysteine protease of Trypanosoma cruzi: a sulfated glycoprotein antigen as relevant candidate for vaccine development and drug target. A review (2009) Curr Med Chem, 16, pp. 3174-3202
  • Duschak, V.G., Couto, A.S., Targets and patented drugs for chemotherapy of Chagas disease (2010) Frontiers in Anti-Infective Drug Discovery, 1, pp. 323-408. , In Atta-ur-Rahman FRS & Choudhary MI (eds):, Chapter 18. Bentham Science
  • Neu, N., Rose, N.R., Beisel, K.W., Herskowitz, A., Gurri-Glass, G., Craig, S.W., Cardiac myosin induces myocarditis in genetically predisposed mice (1987) J Immunol, 139, pp. 3630-3636
  • Tibbetts, R.S., McCormick, T.S., Rowland, E.C., Miller, S.D., Engman, D.M., Cardiac antigen-specific autoantibody production is associated with cardiomyopathy in Trypanosoma cruzi-infected mice (1994) J Immunol, 152, pp. 1493-1499
  • Cunha-Neto, E., Coelho, V., Guilherme, L., Fiorelli, A., Stolf, N., Kalil, J., Autoimmunity in Chagas disease. Identification of cardiac myosin-B13 Trypanosoma cruzi protein cross-reactive T cell clones in heart lesions of a chronic Chagas' cardiomyopathy patient (1996) J Clin Invest, 98, pp. 1709-1712
  • Rizzo, L.V., Cunha-Neto, E., Teixeira, A.R., Autoimmunity in Chagas disease: specific inhibition of reactivity of CD4+ T cells against myosin in mice chronically infected with Trypanosoma cruzi (1989) Infect Immun, 57, pp. 2640-2644
  • Leon, J.S., Godsel, L.M., Wang, K., Engman, D.M., Cardiac myosin autoimmunity in acute Chagas' heart disease (2001) Infect Immun, 69, pp. 5643-5649
  • Motran, C.C., Fretes, R.E., Cerbán, F.M., Rivarola, H.W., Vottero de Cima, E., Immunization with the C-terminal region of Trypanosoma cruzi ribosomal P1 and P2 proteins induces long-term duration cross-reactive antibodies with heart functional and structural alterations in young and aged mice (2000) Clin Immunol, 97, pp. 89-94
  • Giordanengo, L., Maldonado, C., Rivarola, H.W., Induction of antibodies reactive to cardiac myosin and development of heart alterations in cruzipain-immunized mice and their offspring (2000) Eur J Immunol, 30, pp. 3181-3189
  • Leon, J.S., Daniels, M.D., Toriello, K.M., Wang, K., Engman, D.M., A cardiac myosin specific autoimmune response is induced by immunization with Trypanosoma cruzi proteins (2004) Infect Immun, 72, pp. 3410-3417
  • Acosta, D.M., Arnaiz, M.R., Esteva, M.I., Sulfates are main targets of immune responses to cruzipain and are involved in heart damage in BALB/c immunized mice (2008) Int Immunol, 20, pp. 461-470
  • Vosseller, K., Wells, L., Lane, M.D., Hart, G.W., Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes (2002) Proc Natl Acad Sci U S A, 99, pp. 5313-5318
  • Wells, L., Hart, G.W., O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar (2003) FEBS Lett, 546, pp. 154-158. , Review
  • Hedou, J., Cieniewski-Bernard, C., Leroy, Y., Michalski, J.C., Mounier, Y., Bastide, B., O-linked N-acetylglucosaminylation is involved in the Ca2+ activation properties of rat skeletal muscle (2007) J Biol Chem, 282, pp. 10360-10369
  • Comer, F.I., Hart, G.W., O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate (2000) J Biol Chem, 275, pp. 29179-29182. , Review
  • Arnold, C.S., Johnson, G.V., Cole, R.N., Dong, D.L., Lee, M., Hart, G.W., The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine (1996) J Biol Chem, 271, pp. 28741-28744
  • Yao, P.J., Coleman, P.D., Reduction of O-linked N-acetylglucosamine modified assembly protein-3 in Alzheimer's disease (1998) J Neurosci, 18, pp. 2399-23411
  • Slawson, C., Pidala, J., Potter, R., Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins (2001) Biochim Biophys Acta, 1537, pp. 147-157
  • Chou, T.Y., Hart, G.W., Dang, C.V., c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas (1995) J Biol Chem, 270, pp. 18961-18965
  • Juang, Y.T., Solomou, E.E., Rellahan, B., Tsokos, G.C., Phosphorylation and O-linked glycosylation of Elf-1 leads to its translocation to the nucleus and binding to the promoter of the TCR zeta-chain (2002) J Immunol, 168, pp. 2865-2871
  • Wang, Z., Park, K., Comer, F., Hsieh-Wilson, L.C., Saudek, C.D., Hart, G.W., Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes (2009) Diabetes, 58, pp. 309-317
  • Pette, D., Historical perspectives: plasticity of mammalian skeletal muscle (2001) J Appl Physiol, 90, pp. 1119-1124
  • Cieniewski-Bernard, C., Bastide, B., Lefebvre, T., Lemoine, J., Mounier, Y., Michalski, J.C., Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry (2004) Mol Cell Proteomics, 3, pp. 577-585
  • Barboza, M., Duschak, V.G., Cazzulo, J.J., de Lederkremer, R.M., Couto, A.S., Presence of sialic acid in N-linked oligosaccharide chains and O-linked N-acetylglucosamine in cruzipain, the major cysteine proteinase of Trypanosoma cruzi (2003) Mol Biochem Parasitol, 126, pp. 293-296
  • Spinella, S., Liegeard, P., Honte Beyrie-joskowics, M., Trypanosoma cruzi: predominance of Ig2a in nonspecific humoral response during experimental Chagas disease (1992) Exp Parasitol, 74, pp. 46-56
  • Van Parijs, L.V., Peterson, D.A., Abbas, A.K., The Fas/Fas ligand pathway and Bcl-2 regulate T cell responses to model self and foreign antigens (1998) Immunity, 8, pp. 265-274
  • Hu, Y., Suarez, J., Fricovsky, E., Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose (2009) J Biol Chem, 284, pp. 547-555
  • Lori, J., Albert, M.D., Robert, D., Inmanm, D., Molecular mimicry and autoimmunity mechanisms of disease (1999) N Engl J Med, 341, pp. 2068-2074. , Franklin H & Epstein MD (eds)
  • Zachara, N.E., Hart, G.W., The emerging significance of O-GlcNAc in cellular regulation (2002) Chem Rev, 102, pp. 431-438
  • Cunningham, M.W., Autoimmunity and molecular mimicry in the pathogenesis of post-streptococcal heart disease (2003) Front Biosci, 8, pp. 533-543
  • Guilherme, L., Kalil, J., Cunningham, M., Molecular mimicry in the autoimmune pathogenesis of rheumatic heart disease (2006) Autoimmunity, 39, pp. 31-39

Citas:

---------- APA ----------
Acosta, D.M., Soprano, L.L., Ferrero, M., Landoni, M., Esteva, M.I., Couto, A.S. & Duschak, V.G. (2011) . A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin. Parasite Immunology, 33(7), 363-370.
http://dx.doi.org/10.1111/j.1365-3024.2011.01291.x
---------- CHICAGO ----------
Acosta, D.M., Soprano, L.L., Ferrero, M., Landoni, M., Esteva, M.I., Couto, A.S., et al. "A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin" . Parasite Immunology 33, no. 7 (2011) : 363-370.
http://dx.doi.org/10.1111/j.1365-3024.2011.01291.x
---------- MLA ----------
Acosta, D.M., Soprano, L.L., Ferrero, M., Landoni, M., Esteva, M.I., Couto, A.S., et al. "A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin" . Parasite Immunology, vol. 33, no. 7, 2011, pp. 363-370.
http://dx.doi.org/10.1111/j.1365-3024.2011.01291.x
---------- VANCOUVER ----------
Acosta, D.M., Soprano, L.L., Ferrero, M., Landoni, M., Esteva, M.I., Couto, A.S., et al. A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin. Parasite Immunol. 2011;33(7):363-370.
http://dx.doi.org/10.1111/j.1365-3024.2011.01291.x