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Titolo:
Epitope mapping using the X-ray crystallographic structure of complement receptor type 2 (CR2)/CD21: Identification of a highly inhibitory monoclonalantibody that directly recognizes the CR2-C3d interface
Autore:
Guthridge, JM; Young, K; Gipson, MG; Sarrias, MR; Szakonyi, G; Chen, XJS; Malaspina, A; Donoghue, E; James, JA; Lambris, JD; Moir, SA; Perkins, SJ; Holers, VM;
Indirizzi:
Univ Colorado, Hlth Sci Ctr, Dept Med & Immunol, Denver, CO 80262 USA UnivColorado Denver CO USA 80262 ept Med & Immunol, Denver, CO 80262 USA Univ Colorado, Hlth Sci Ctr, Dept Biochem & Mol Genet, Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 ochem & Mol Genet, Denver, CO 80262 USA Univ Penn, Prot Chem Lab, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Chem Lab, Philadelphia, PA 19104 USA NIAID, Immunoregulat Lab, NIH, Bethesda, MD 20892 USA NIAID Bethesda MD USA 20892 mmunoregulat Lab, NIH, Bethesda, MD 20892 USA Oklahoma Med Res Fdn, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn Oklahoma City OK USA 73104 lahoma City, OK 73104 USA Univ Oklahoma, Hlth Sci Ctr, Oklahoma City, OK 73104 USA Univ Oklahoma Oklahoma City OK USA 73104 Ctr, Oklahoma City, OK 73104 USA Univ Coll London, Royal Free & Univ Coll Med Sch, Dept Biochem & Mol Biol,London, England Univ Coll London London England Dept Biochem & Mol Biol,London, England
Titolo Testata:
JOURNAL OF IMMUNOLOGY
fascicolo: 10, volume: 167, anno: 2001,
pagine: 5758 - 5766
SICI:
0022-1767(20011115)167:10<5758:EMUTXC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPSTEIN-BARR-VIRUS; HUMAN LYMPHOCYTES-B; SYSTEMIC LUPUS-ERYTHEMATOSUS; FOLLICULAR DENDRITIC CELLS; T-DEPENDENT ANTIGEN; CD21 LIGAND-BINDING; CR-2 CD21; ACQUIRED-IMMUNITY; C3D; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Holers, VM Univ Colorado, Hlth Sci Ctr, Dept Med, Box B-115,4200 E 9th Ave, Denver, CO 80262 USA Univ Colorado Box B-115,4200 E 9th Ave Denver CO USA80262 USA
Citazione:
J.M. Guthridge et al., "Epitope mapping using the X-ray crystallographic structure of complement receptor type 2 (CR2)/CD21: Identification of a highly inhibitory monoclonalantibody that directly recognizes the CR2-C3d interface", J IMMUNOL, 167(10), 2001, pp. 5758-5766

Abstract

Complement receptor type 2 (CR2)/CD21 is a B lymphocyte cell membrane C3d/iC3b receptor that plays a central role in the immune response. Human CR2 is also the receptor for the EBV viral membrane glycoprotein gp350/220. BothC3d and gp350/220 bind CR2 within the first two of 15-16 repetitive domains that have been designated short consensus/complement repeats. Many mAbs react with human CR2; however, only one currently available mAb is known to block both C3d/iC3b find gp350/220 binding. We have used a recombinant formof human CR2 containing the short consensus/complement repeat 1-2 ligand-binding fragment to immunize Cr2(-/-) mice. Following fusion, we identified and further characterized four new anti-CR2 mAbs that recognize this fragment. Three of these inhibited binding of CR2 to C3d and gp350/220 in different forms. We have determined the relative inhibitory ability of the four mAbs to block ligand binding, and we have used overlapping peptide-based approaches to identify linear epitopes recognized by the inhibitory mAbs. Placement of these epitopes on the recently solved crystal structure of the CR2-C3d complex reveals that each inhibitory mAb recognizes a site either within or adjacent to the CR2-C3d contact site. One new mAb, designated 171, blocks CR2 receptor-ligand interactions with the greatest efficiency and recognizes a portion of the C3d contact site on CR2. Thus, we have created an anti-human CR2 mAb that blocks the C3d ligand by direct contact with its interaction site, and we have provided confirmatory evidence that the C3d binding site seen in its crystal structure exists in solution.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:00:07