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Titolo:
V(H)3 FAMILY ANTIBODIES BIND DOMAIN-D OF STAPHYLOCOCCAL PROTEIN-A
Autore:
ROBEN PW; SALEM AN; SILVERMAN GJ;
Indirizzi:
UNIV CALIF SAN DIEGO,DEPT MED 0663,THEODORE GILDRED CANC CTR,9500 GILLMAN DR LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,DEPT MED 0663,THEODORE GILDRED CANC CTR LA JOLLACA 92093 UNIV CALIF SAN DIEGO,SAM & ROSE STEIN INST RES AGING LA JOLLA CA 92093
Titolo Testata:
The Journal of immunology
fascicolo: 12, volume: 154, anno: 1995,
pagine: 6437 - 6445
SICI:
0022-1767(1995)154:12<6437:VFABDO>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN-BINDING; AUREUS COWAN; HUMAN-IGM; FC-GAMMA; REGION; GENE; FRAGMENT; ANTIGEN; IDENTIFICATION; STREPTOCOCCI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
P.W. Roben et al., "V(H)3 FAMILY ANTIBODIES BIND DOMAIN-D OF STAPHYLOCOCCAL PROTEIN-A", The Journal of immunology, 154(12), 1995, pp. 6437-6445

Abstract

Staphylococcal protein A (SpA) is a 45-kDa bacterial membrane proteinthat can interact with either Fc gamma, a constant region portion of IgG, or with the Fab portion that also mediates conventional Ag binding. In recent reports, SpA has been shown to specifically interact withFab derived from the V(H)3 family and is little affected by V-H CDR3,J(H), or light chain usage. To identify a site on SpA responsible forV(H)3 Fab binding, we cloned and expressed in Escherichia coli the 61amino acid sequence of SpA that represents domain D, and this small protein exhibited both the V(H)3 Fab and Fc gamma binding specificities. Surface plasmon resonance measurements demonstrated that domain D and native SpA had the strongest binding interactions with an IgM-kappa encoded by the germline configuration of the V(H)3 gene V(H)26c. In contrast, the apparent affinities for Fc gamma binding were at least fivefold weaker. A variant of domain D was also created that is devoid ofthe three-codon insertion that distinguishes domain D from all other domains in SpA. Although this deletion did not significantly affect the V(H)3 Fab-mediated SpA binding activity, it did improve the affinityof Fc gamma binding by an order of magnitude. These observations characterize a site on SpA responsible for binding interactions with B cell Ag receptors that are highly analogous to that of superantigens for T cell receptors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 22:15:22