Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Hybrid IgA2/IgG1 antibodies with tailor-made effector functions
Autore:
Chintalacharuvu, KR; Vuong, LUC; Loi, LA; Larrick, JW; Morrison, SL;
Indirizzi:
Univ Calif Los Angeles, Dept Microbiol Mol Genet & Immunol, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Plant Biotechnol Inc, Mt View, CA 94043 USA Plant Biotechnol Inc Mt View CA USA 94043 hnol Inc, Mt View, CA 94043 USA
Titolo Testata:
CLINICAL IMMUNOLOGY
fascicolo: 1, volume: 101, anno: 2001,
pagine: 21 - 31
SICI:
1521-6616(200110)101:1<21:HIAWTE>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
FC RECEPTOR; J-CHAIN; COMPLEMENT ACTIVATION; CHIMERIC ANTIBODY; BINDING-AFFINITY; IMMUNOGLOBULIN-G; CONSTANT-REGION; DOMAIN; IGG;
Keywords:
polymeric Igs; hybrid antibodies; FcRn binding; serum half-life; complement activation; Fc receptor binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Chintalacharuvu, KR Univ Calif Los Angeles, Dept Microbiol Mol Genet & Immunol, 405 Hilgard Ave, Los Angeles, CA 90095 USA Univ Calif Los Angeles 405Hilgard Ave Los Angeles CA USA 90095
Citazione:
K.R. Chintalacharuvu et al., "Hybrid IgA2/IgG1 antibodies with tailor-made effector functions", CLIN IMMUNO, 101(1), 2001, pp. 21-31

Abstract

Immunoglobulin (Ig) A and IgG are the principal immune effector molecules at mucosal surfaces and in blood, respectively. Mucosal IgA is polymeric and bound to secretory component, whereas serum IgG is monomeric. We have nowproduced IgA2/IgG1 hybrid antibodies that combine the properties of IgA and IgG. Antibodies with C(alpha)3 at the end of the IgG H chain resemble IgAand form polymers with J chain that bind the polymeric Ig receptor. Like IgG, the hybrid proteins activated complement and bound Fc gamma RI and protein A. Though the hybrid proteins contained both C(gamma)2 and C(gamma)3, they have a short in vivo half-life. Surprisingly, this decreased half-life correlated with a higher avidity than that of IgG for murine FcRn. Interestingly, antibodies with C(alpha)1 replacing C(gamma)1 were resistant to extremes of pH, suggesting that C(alpha)1 increases antibody stability. These results provide insights into engineering antibodies with novel combinationsof effector functions. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:19:09