Presence of sialic acid in N-linked oligosaccharide chains and O-linked N-acetylglucosamine in cruzipain, the major cystein proteinase of Trypanosoma cruzi

MARIANA BARBOZA; VILMA G. DUSCHAK; JUAN J. CAZZULO; ROSA M. DE LEDERKREMER; ALICIA S. COUTO

MOLECULAR AND BIOCHEMICAL PARASITOLOGY

Elsevier/North-Holland Biomedical Press

Lugar: Netherlands; Año: 2003 vol. 127 p. 69 - 72

0166-6851

Cruzipain is the major cysteine proteinase (CP) of Trypanosoma cruzi, the parasitic protozoan causing the American trypanosomiasis, Chagas disease [1]. The enzyme is present at high levels in the epimastigote form, and at lower levels in the other stages of the parasite’s life cycle [2]. Mature cruzipain consists of a catalytic moiety, homologous to papain and mammalian cathepsins S and L, the parasitic protozoan causing the American trypanosomiasis, Chagas disease [1]. The enzyme is present at high levels in the epimastigote form, and at lower levels in the other stages of the parasite’s life cycle [2]. Mature cruzipain consists of a catalytic moiety, homologous to papain and mammalian cathepsins S and L[1]. The enzyme is present at high levels in the epimastigote form, and at lower levels in the other stages of the parasite’s life cycle [2]. Mature cruzipain consists of a catalytic moiety, homologous to papain and mammalian cathepsins S and L[2]. Mature cruzipain consists of a catalytic moiety, homologous to papain and mammalian cathepsins S and L [1], and a C-terminal domain (C-T). The latter is present in all Type I CPs from Trypanosomatids [3] at variance with the other CPs reported so far; its function is still unknown [1]., and a C-terminal domain (C-T). The latter is present in all Type I CPs from Trypanosomatids [3] at variance with the other CPs reported so far; its function is still unknown [1].[3] at variance with the other CPs reported so far; its function is still unknown [1].[1].