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Titolo:
Identification of a peptide that protects the human acetylcholine receptoragainst antigenic modulation
Autore:
Luo, GX; Victor, K; Chong, K; McNeeley, P; Ramirez, D; Preclaro, J; Linnik, MD; Campbell, MA;
Indirizzi:
La Jolla Pharmaceut Co, San Diego, CA 92121 USA La Jolla Pharmaceut Co San Diego CA USA 92121 Co, San Diego, CA 92121 USA
Titolo Testata:
JOURNAL OF IMMUNOLOGICAL METHODS
fascicolo: 1-2, volume: 251, anno: 2001,
pagine: 177 - 186
SICI:
0022-1759(20010501)251:1-2<177:IOAPTP>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAIN IMMUNOGENIC REGION; AUTOIMMUNE MYASTHENIA-GRAVIS; CELL-LINE TE671; MONOCLONAL-ANTIBODIES; PASSIVE TRANSFER; FAB FRAGMENTS; BINDING SITE; PHAGE; AUTOANTIBODIES; SPECIFICITIES;
Keywords:
autoimmunity; antigens/peptides/epitope; phage display; myasthenia gravis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Campbell, MA La Jolla Pharmaceut Co, 6455 Nancy Ridge Dr, San Diego, CA 92121 USA La Jolla Pharmaceut Co 6455 Nancy Ridge Dr San Diego CA USA 92121
Citazione:
G.X. Luo et al., "Identification of a peptide that protects the human acetylcholine receptoragainst antigenic modulation", J IMMUNOL M, 251(1-2), 2001, pp. 177-186

Abstract

mAb 192 is a rat monoclonal antibody with very high affinity for the majorimmunogenic region (MIR) of the human muscle acetylcholine receptor (AChR). An epitope mimic of this antibody was selected from a phage display peptide library screened with mAb 192. The peptide-presenting phage has been shown to specifically bind to solid phase mAb 192 with an equilibrium dissociation constant (K-d) of 8.45x10(-9) M, as directly measured with surface plasmon resonance. This value represents the avidity of the interaction between selected phage and mAb 192. A synthetic version of this peptide QPSPYNGWRMEI, referred to as MG15, binds to its selecting antibody and blocks the interaction of mAb 192 with human AChR. Peptide MG15 was able to protect acetylcholine receptors on human RD cells from antibody-mediated down-modulation. The negative charge of glutamic acid plays a important role in antibody binding. Replacement of the glutamic acid with an alanine completely abolishes the inhibitory activity. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 21:48:28