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Titolo:
Binding specificity of mannose-specific carbohydrate-binding protein from the cell surface of Trypanosoma cruzi
Autore:
Bonay, P; Molina, R; Fresno, M;
Indirizzi:
Autonomous Univ Madrid, Ctr Biol Mol Severo Ochoa, Madrid, Spain Autonomous Univ Madrid Madrid Spain iol Mol Severo Ochoa, Madrid, Spain Inst Salud Carlos III, Ctr Nacl Microbiol, Madrid, Spain Inst Salud CarlosIII Madrid Spain I, Ctr Nacl Microbiol, Madrid, Spain
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 9, volume: 11, anno: 2001,
pagine: 719 - 729
SICI:
0959-6658(200109)11:9<719:BSOMCP>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BUG TRIATOMA-INFESTANS; WHEAT-GERM-AGGLUTININ; ULTRAVIOLET DIFFERENCE SPECTROSCOPY; SCANNING ELECTRON-MICROSCOPY; CHAGAS-DISEASE; N-ACETYLGLUCOSAMINE; CONCANAVALIN-A; PEANUT AGGLUTININ; HOST-CELLS; AUTOIMMUNITY;
Keywords:
Trypanosoma cruzi; carbohydrate-binding protein; mannose-specific;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Bonay, P Autonomous Univ Madrid, Ctr Biol Mol Severo Ochoa, Madrid, Spain Autonomous Univ Madrid Madrid Spain evero Ochoa, Madrid, Spain
Citazione:
P. Bonay et al., "Binding specificity of mannose-specific carbohydrate-binding protein from the cell surface of Trypanosoma cruzi", GLYCOBIOLOG, 11(9), 2001, pp. 719-729

Abstract

The sugar binding specificity of the recently described mannose-specific carbohydrate-binding proteins (CBP) isolated to homogeneity from both the epimastigote and trypomastigote stages of the pathogenic protozoa Trypanosomacruzi has been studied by quantitative hapten inhibition of the biotinylated CBPs to immobilized thyroglobulin using model oligosaccharides. The results clearly show a differential specificity toward high-mannose glycans between the CBPs from the two developmental stages. Thus, the isolated CBP from epimastigotes exhibited stronger affinity for higher mannose oligomers containing the Man alpha1-2Man alpha1-6Man alpha1-6 structure. Its affinity decreased, as did the number of mannose residues on the oligomer orremoval of the terminal Man alpha1-2-linked mannose. By contrast the CBP isolated from the trypomastigote stage showed about 400-fold lower avidity than the epimastigote form, and contrary to it, it was slightly more specific toward Man(5)GlcNAc than Man(9)GlcNAc. Analysis of the interaction of epimastigote-Man-CBP with its ligands by UV difference spectroscopy indicates the existence of an extended binding site in that protein with a large enthalpic contribution to the binding. The thermodynamic parameters of binding were obtained by isothermal titration calorimetry and been found that the DeltaH values to be in good agreement with the van't Hoff values. The binding reactions are mainly enthalpically driven and exhibit enthalpy-enthropy compensation. In addition, analysis of the high-mannose glycans from different parts of the digestive tract of the reduviid insect vector of T. cruzi suggest a role of the CBP in the retention of the epimastigote stage in the anterior portion of the gut.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/10/17 alle ore 11:10:06