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Glycobiology, 2000, Vol. 10, No. 5 459-465
© 2000 Oxford University Press

Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes

Flor Porras2, Ricardo Lascurain3, Raúl Chávez3, Blanca Ortiz2, Pedro Hernández2, Henri Debray4 and Edgar Zenteno1,3

2Departamento de Bioquímica, Instituto Nacional de Enfermedades Respiratorias, Calzada de Tlalpan 4502, 01040 México, 3Laboratorio de Inmunología, Departamento de Bioquímica, Facultad de Medicina, UNAM, 04510, México, and 4Laboratoire de Chimie Biologique de la Université des Sciences et Technologies de Lille, UMR du CNRS n° 8576, Villeneuve d’Ascq, 59655 France

From murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL+ thymocytes (83%) are naive cells with the CD4+CD8-CD45RB+ phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor’s peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (<17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-ß type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells.

1 To whom correspondence should be addressed at: Laboratorio de Inmunologia, Departamento de Bioquimica, Facultad de Medicina UNAM, PO Box 70159, 04510 Mexico


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