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Titolo:
CONGO-RED BINDING BY PORPHYROMONAS-GINGIVALIS IS MEDIATED BY A 66-KDAOUTER-MEMBRANE PROTEIN
Autore:
SMALLEY JW; BIRSS AJ; MCKEE AS; MARSH PD;
Indirizzi:
UNIV LIVERPOOL,SCH DENT,DEPT CLIN DENT SCI,ORAL BIOL UNIT LIVERPOOL L69 3BX MERSEYSIDE ENGLAND PUBL HLTH LAB SERV,CTR APPL MICROBIOL & RES,DIV RES SALISBURY SP4 0JGWILTS ENGLAND
Titolo Testata:
Microbiology
, volume: 141, anno: 1995,
parte:, 1
pagine: 205 - 211
SICI:
1350-0872(1995)141:<205:CBBPIM>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
IRON TRANSPORT PROTEINS; HEMIN-BINDING; BACTEROIDES-GINGIVALIS; SURFACE PROTEIN; AEROMONAS-SALMONICIDA; SHIGELLA-FLEXNERI; VIRULENCE; W50; GROWTH; PORPHYROMONAS-(BACTEROIDES)-GINGIVALIS;
Keywords:
PORPHYROMONAS GINGIVALIS; LIGAND BINDING; CONGO RED; HEMIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
J.W. Smalley et al., "CONGO-RED BINDING BY PORPHYROMONAS-GINGIVALIS IS MEDIATED BY A 66-KDAOUTER-MEMBRANE PROTEIN", Microbiology, 141, 1995, pp. 205-211

Abstract

Congo red was bound from solution by strains of Porphyromonas gingivalis including W50, HG189, HC184 NCTC 11834 Bg 381, WPH35, the slower brown pigmenting colonial variant W50/BR1, and the avirulent mutant W50/BE1, and by Porphyromonas endodontalis HC370 and Porphyromonas asaccharolytica B537. SDS-PACE of whole cells of all species examined displayed a 66 kDa Congo-red-binding component which was also detected in the outer membranes of P. gingivalis W50 grown in the chemostat under both haemin limitation and haemin excess, and which corresponded to a Coomassie-blue-stained band of the same mobility. Pretreatment of haemin-excess batch-grown cells of P. gingivalis W50 with polymyxin B, whichbinds to lipid A, did not inhibit binding, whilst binding was enhanced in the presence of 2 M ammonium sulphate, suggesting the involvementof non-specific hydrophobic interactions. Binding was also reduced bypretreatment with trypsin and papain, and by 8-anilino-1-naphthalenesulphonic acid, which binds to hydrophobic amino acids. The 66 kDa binding component was sensitive to proteinase K digestion, and loss of Congo red staining of this band correlated with the quantitative reduction in Congo red binding by whole cells. These data, and our previous work, show that Congo red and iron protoporphyrin IX (haemin) are bound to different outer-membrane components, and that Congo red binding maybe of little value as a marker to detect virulent strains of P. gingivalis or those expressing haemin-binding proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:54:19