TAILIEUCHUNG - Báo cáo khoa học: Structural analysis of the N-glycans of the major cysteine proteinase of Trypanosoma cruzi Identification of sulfated high-mannose type oligosaccharides

Trypanosoma cruzi, the parasitic protozoan that causes Chagas disease, contains a major cysteine proteinase, cruzipain. This lysosomal enzyme bears an unusual C-terminal extension that contains a number of post-translational modifications, and most antibodies in natural and experimen-tal infections are directed against it. In this report we took advantage of UV-MALDI-TOF mass spectrometry in conjunction with peptide N-gly-cosidase F deglycosylation and high performance anion exchange chroma-tography analysis to address the structure of the N-linked oligosaccharides present in this domain. . | ềFEBS Journal Structural analysis of the N-glycans of the major cysteine proteinase of Trypanosoma cruzi Identification of sulfated high-mannose type oligosaccharides Mariana Barboza1 Vilma G. Duschak2 Yuko Fukuyama Hiroshi Nonami3 Rosa Erra-Balsells4 Juan J. Cazzulo1 and Alicia S. Couto4 1 Institute de Investigaciones Biotecnologicas-INTECH Universidad Nacionalde Gral. San Martin Buenos Aires Argentina 2 Instituto Nacionalde Parasitologia Dr Mario Fatala Chaben ANLIS Ministerio de Salud y Ambiente Buenos Aires Argentina 3 College of Agriculture Ehime University Matsuyama Japan 4 CIHIDECAR CONICET Departamento de Quimica Organica Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires Argentina Keywords Cruzipain nor-harmane sulfated oligosaccharides Trypanosoma cruzi UV-mAldi-tof ms Correspondence A. S. Couto CIHIDECAR CONICET Departamento de Quimica Orgai nica Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires Buenos Aires CP 1428 Argentina Fax 54 11 45763346 Tel 54 11 45763346 E-mail acouto@ Present address Koichi Tanaka Mass Spectrometry Research Laboratory Shimadzu Corporation 1 Nishinokyo-Kuwabaracho Nakagyo-ku Kyoto 604-8511 Japan Received 8 April2005 accepted 23 May 2005 doi Trypanosoma cruzi the parasitic protozoan that causes Chagas disease contains a major cysteine proteinase cruzipain. This lysosomal enzyme bears an unusual C-terminal extension that contains a number of post-translational modifications and most antibodies in natural and experimental infections are directed against it. In this report we took advantage of UV-MALDI-TOF mass spectrometry in conjunction with peptide N-gly-cosidase F deglycosylation and high performance anion exchange chromatography analysis to address the structure of the N-linked oligosaccharides present in this domain. The UV-MALDI-TOF MS analysis in the negativeion mode using nor-harmane as matrix allowed us to determine a new striking feature .

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