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Titolo:
CHARACTERIZATION OF THE PORPHYROMONAS-GINGIVALIS ANTIGEN RECOGNIZED BY A MONOCLONAL-ANTIBODY WHICH PREVENTS COLONIZATION BY THE ORGANISM
Autore:
BOOTH V; LEHNER T;
Indirizzi:
UNITED MED & DENT SCH,GUYS & ST THOMAS HOSP,DEPT PERIODONTOL & PREVENT DENT,FLOOR 21 LONDON SE1 9RT ENGLAND UNITED MED & DENT SCH,GUYS & ST THOMAS HOSP,DEPT IMMUNOL LONDON SE1 9RT ENGLAND
Titolo Testata:
Journal of Periodontal Research
fascicolo: 1, volume: 32, anno: 1997,
parte:, 1
pagine: 54 - 60
SICI:
0022-3484(1997)32:1<54:COTPAR>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; STREPTOCOCCUS-MUTANS; PERIODONTAL-DISEASES; W50; HEMAGGLUTININ; ACTINOMYCETEMCOMITANS; IMMUNIZATION; EXPRESSION; PROTEASES; PROTEINS;
Keywords:
MONOCLONAL ANTIBODY; PORPHYROMONAS-GINGIVALIS; HEMAGGLUTININ; COLONIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
V. Booth e T. Lehner, "CHARACTERIZATION OF THE PORPHYROMONAS-GINGIVALIS ANTIGEN RECOGNIZED BY A MONOCLONAL-ANTIBODY WHICH PREVENTS COLONIZATION BY THE ORGANISM", Journal of Periodontal Research, 32(1), 1997, pp. 54-60

Abstract

Monoclonal antibody (MAb) 61BG1.3 prevented recolonization of deep pockets by Porphyromonas gingivalis in patients with periodontitis. The aim of this work was to identify the antigen recognized by the MAb. This was carried out by dose-dependent inhibition with materials extracted from P. gingivalis and assessed by a radioimmunoassay. A protease preparation and a capsular extract inhibited about 95% of the binding activity, whereas LPS or fimbriae had no effect. However, about 125 times greater concentration of the capsular than the protease material was needed to inhibit 50% of the antibody activity, suggesting that the MAb recognizes the protease preparation and that the capsular extract contained some protease. Western blotting of MAb 61BG1.3 with recombinant prpRI protein expressed in Escherichia coli confirmed that MAb 61BG1.3 recognizes the haemagglutinating protease and mapped its epitope to residues 748-1130 of the beta component of the polyprotein. Three major bands of M(r) 45,000, 38,300 and 31,400 were detected in native whole cells of the virulent P. gingivalis strain W50 by Western blotting with MAb 61BG1.3. The MAb inhibited haemagglutination of human red blood cells by P. gingivalis or by a native protease extract. Blocking adhesion of P. gingivalis to the receptors on erythrocytes might be a mechanism by which the MAb inhibits recolonization by the microorganism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:46:01