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Titolo:
CHARACTERIZATION OF A MONOCLONAL-ANTIBODY DIRECTED AGAINST THE NH2 TERMINAL AREA OF INTERLEUKIN-2 (IL-2) AND INHIBITING SPECIFICALLY THE BINDING OF IL-2 TO IL-2 RECEPTOR-BETA CHAIN (IL-2R-BETA)
Autore:
MOREAU JL; BOSSUS M; DEGROOTE D; FRANCOIS C; JACQUES Y; TARTAR A; THEZE J;
Indirizzi:
INST PASTEUR,UNITE IMMUNOGENET CELLULAIRE,25 RUE DR ROUX F-75015 PARIS FRANCE INST PASTEUR,UNITE IMMUNOGENET CELLULAIRE F-75015 PARIS FRANCE INST PASTEUR,CNRS,URA 1309,UNITE CHIM BIOMOLEC F-59000 LILLE FRANCE INST BIOL,INSERM,U211 F-44035 NANTES FRANCE
Titolo Testata:
Molecular immunology
fascicolo: 14-15, volume: 32, anno: 1995,
pagine: 1047 - 1056
SICI:
0161-5890(1995)32:14-15<1047:COAMDA>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-CELL LINES; HIGH-AFFINITY; ALPHA-CHAIN; AMINO-ACID; MOUSE INTERLEUKIN-2; EXPRESSION; P55; IDENTIFICATION; RESIDUES; INDUCTION;
Keywords:
IL-2; IL-2 RECEPTOR; ANTI-IL-2 MAB;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
J.L. Moreau et al., "CHARACTERIZATION OF A MONOCLONAL-ANTIBODY DIRECTED AGAINST THE NH2 TERMINAL AREA OF INTERLEUKIN-2 (IL-2) AND INHIBITING SPECIFICALLY THE BINDING OF IL-2 TO IL-2 RECEPTOR-BETA CHAIN (IL-2R-BETA)", Molecular immunology, 32(14-15), 1995, pp. 1047-1056

Abstract

An anti-human IL-2 mAb (19B11/beta) was found to selectively block the binding of IL-2 to TS1 beta cells expressing the interleukin-2 receptor beta (IL-2R beta) without affecting binding to TSl alpha: cells expressing the IL-2R alpha receptor. It also specifically inhibits the IL-2 driven cell proliferation in TSl beta cells. These observations have lead to the hypothesis that its epitope is related to an IL-2 area involved in binding with IL-2R beta chain. This epitope was identifiedusing various peptides covering the N-terminal half (including alpha helix A) of the 133 amino acids of IL-2. MAb 19B11/beta does not recognize peptides 30-54 and 44-54 but recognizes peptides 1-22 and 1-30 with a good affinity. Furthermore, threonine in position no. 3 was foundto be critical for the binding of mAb 19B11/beta. A relationship between the epitope of mAb 19B11/beta and the glycosylation of the IL-2 molecule was observed. This further demonstrates that the NH, terminal area of IL-2 is critical for IL-2/IL-2R beta interactions. Two other mAbs were studied during the course of this work. They served as controlfor the study of mAb 19B11/beta and provide some additional insight concerning the question of IL-2/IL-2R structure-function. MAb 16F11/alpha selectively blocks the IL-2 binding to TS1 alpha cells. The epitopeof mAb 16F11 is conformational and it was not possible to study the corresponding IL-2/IL-2R alpha region of interaction. Epitope of mAb 3H9 is localized between residues 30 and 54 and does not affect the binding of IL-2 to IL-2R alpha.

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Documento generato il 22/01/20 alle ore 06:31:40