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Titolo:
THE NATURAL HUMAN-IGG ANTI-F(AB')(2) ANTIBODY RECOGNIZES A CONFORMATIONAL IGG1 HINGE EPITOPE
Autore:
TERNESS P; KOHL I; HUBENER G; BATTISTUTTA R; MORODER L; WELSCHOF M; DUFTER C; FINGER M; HAIN C; JUNG M; OPELZ G;
Indirizzi:
UNIV HEIDELBERG,INST IMMUNOL,DEPT TRANSPLANTAT IMMUNOL,INF 305 D-69120 HEIDELBERG GERMANY MAX PLANCK INST BIOCHEM W-8033 MARTINSRIED GERMANY
Titolo Testata:
The Journal of immunology
fascicolo: 12, volume: 154, anno: 1995,
pagine: 6446 - 6452
SICI:
0022-1767(1995)154:12<6446:TNHAAR>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
FULLY SYNTHETIC IMMUNOGENS; NUCLEAR MAGNETIC-RESONANCE; IMMUNOGLOBULIN-G; IDIOTYPIC ANTIBODIES; FRAGMENT 225-232; B-CELLS; ALLOIMMUNIZATION; REGION; ASSOCIATION; FLEXIBILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
P. Terness et al., "THE NATURAL HUMAN-IGG ANTI-F(AB')(2) ANTIBODY RECOGNIZES A CONFORMATIONAL IGG1 HINGE EPITOPE", The Journal of immunology, 154(12), 1995, pp. 6446-6452

Abstract

Natural IgG anti-F(ab')(2) Abs are part of the physiologic immune repertoire and have important immunoregulatory functions. Although previous work suggested that some of these Abs recognize epitopes located inthe constant region of the F(ab')(2) molecule, an exact epitope mapping has not been performed. We found that the anti-F(ab')(2) Ab binds strongly to F(ab')(2) but only weakly to Fab fragments. Fab fragments are lacking the core and lower hinge region. In our experiments, we show that the IgG anti-F(ab')(2) Ab binds strongly to a synthetic double chain peptide (225-237/225'-237') comprising the core and lower hinge region of the human IgG1 molecule. In contrast, it binds only weakly to the same peptide in monomeric form (225-237) or to a short double chain hinge peptide (225-232/225'-232'). The double chain peptides comprise a cyclic region between the two cystine bridges and an exocyclic region. Previous nuclear magnetic resonance analyses showed that the cyclic portion of the short double chain hinge peptide adopts the same conformation as that found in the intact IgG1 molecule. The dichroic properties of the short and long double chain hinge peptides indicate that they have identical conformations in their cyclic regions, but havedifferent conformations in their exocyclic regions. The conformational differences in the exocyclic regions explain the binding of the Ab to the long double chain hinge peptide and the lack of binding to the short one. The circular dichroism spectrum of the monomeric hinge peptide, which is not recognized by the Ab, is consistent with the absence of an ordered peptide structure. These findings lead us to conclude that the IgG anti-F(ab')(2) Ab recognizes a conformational IgG1 hinge epitope.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 12:28:26