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Titolo:
Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase
Autore:
McGraw, WT; Potempa, J; Farley, D; Travis, J;
Indirizzi:
Univ Georgia, Dept Biochem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 rgia, Dept Biochem, Athens, GA 30602 USA Nova Pharmaceut Corp, Dept Arthrit Biol, Summit, NJ 07901 USA Nova Pharmaceut Corp Summit NJ USA 07901 thrit Biol, Summit, NJ 07901 USA Jagiellonian Univ, Inst Mol Biol, Krakow, Poland Jagiellonian Univ Krakow Poland ian Univ, Inst Mol Biol, Krakow, Poland
Titolo Testata:
INFECTION AND IMMUNITY
fascicolo: 7, volume: 67, anno: 1999,
pagine: 3248 - 3256
SICI:
0019-9567(199907)67:7<3248:PCASAO>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
VASCULAR-PERMEABILITY ENHANCEMENT; BACTEROIDES-GINGIVALIS; CYSTEINE PROTEINASE; CREVICULAR FLUID; PERIODONTITIS; ARGININE; MICROFLORA; DEGRADATION; GENERATION; KALLIKREIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Travis, J Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA UnivGeorgia Athens GA USA 30602 Mol Biol, Athens, GA 30602 USA
Citazione:
W.T. McGraw et al., "Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase", INFEC IMMUN, 67(7), 1999, pp. 3248-3256

Abstract

The initiation and progression of adult-onset periodontitis has been associated with infection of the gingival sulcus by Porphyromonas gingivalis. This organism utilizes a multitude of virulence factors to evade host defenses as it establishes itself as one of the predominant pathogens in periodontal pockets. A feature common to many other oral pathogens is the productionof ammonia due to its protective effect during acidic cleansing cycles in the mouth. Additionally, ammonia production by P. gingivalis has been proposed as a virulence factor due to its negative effects on neutrophil function. In this study, we describe the first purification of a peptidyl argininedeiminase (PAD) from a prokaryote. PAD exhibits biochemical characteristics and properties that suggest that it may be a virulence agent. PAD deiminates the guanidino group of carboxyl-terminal arginine residues on a varietyof peptides, including the vasoregulatory peptide-hormone bradykinin, to yield ammonia and a citrulline residue. The soluble protein has an apparent mass of 46 kDa, while the DNA sequence predicts a full-length protein of 61.7 kDa. PAD is optimally active at 55 degrees C, stable at low pH, and shows the greatest activity above pH 9.0. Interestingly, in the presence of stabilizing factors, PAD is resistant to limited proteolysis and retains significant activity after short-term boiling. We propose that PAD, acting in concert with arginine-specific proteinases from P. gingivalis, promotes the growth of the pathogen In the periodontal pocket, initially by enhancing itssurvivability and then by assisting the organism in its circumvention of host humoral defenses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 10:02:28