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Titolo:
Porphyrin-mediated binding to hemoglobin by the HA2 domain of cysteine proteinases (gingipains) and hemagglutinins from the periodontal pathogen Porphyromonas gingivalis
Autore:
DeCarlo, AA; Paramaesvaran, M; Yun, PLW; Collyer, C; Hunter, N;
Indirizzi:
Univ Alabama, Sch Dent, Dept Periodont, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Periodont, Birmingham, AL 35294 USA Univ Alabama, Dept Oral Biol, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Oral Biol, Birmingham, AL 35294 USA Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney SydneyNSW Australia 2006 iochem, Sydney, NSW 2006, Australia Inst Dent Res, Sydney, NSW, Australia Inst Dent Res Sydney NSW AustraliaInst Dent Res, Sydney, NSW, Australia
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 12, volume: 181, anno: 1999,
pagine: 3784 - 3791
SICI:
0021-9193(199906)181:12<3784:PBTHBT>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; HEMIN-BINDING; PERIODONTOPATHOGENIC BACTERIA; MATRIX METALLOPROTEINASES; PROTOPORPHYRIN-IX; CREVICULAR FLUID; GNOTOBIOTIC-RATS; MULTIPLE FORMS; LYS-GINGIPAIN; PROTEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: DeCarlo, AA Univ Alabama, Sch Dent, Dept Periodont, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Birmingham, AL 35294 USA
Citazione:
A.A. DeCarlo et al., "Porphyrin-mediated binding to hemoglobin by the HA2 domain of cysteine proteinases (gingipains) and hemagglutinins from the periodontal pathogen Porphyromonas gingivalis", J BACT, 181(12), 1999, pp. 3784-3791

Abstract

Heme binding and uptake are considered fundamental to the growth and virulence of the gram-negative periodontal pathogen Porphyromonas gingivalis. Wetherefore examined the potential role of the dominant P. gingivalis cysteine proteinases (gingipains) in the acquisition of heme from the environment, A recombinant hemoglobin-binding domain that is conserved between two predominant gingipains (domain HA2) demonstrated tight binding to hemin (K-d =16 nM), and binding was inhibited by iron-free protoporphyrin IX (K-i = 2.5 mu M). Hemoglobin binding to the gingipains and the recombinant HA2 (rHA2) domain (K-d = 2.1 nM) was also inhibited by protoporphyrin IX (K-i 10 mu M), demonstrating an essential interaction between the HA2 domain and the heme moiety in hemoglobin binding. Binding of rHA2 with either hemin, protoporphyrin IX, or hematoporphyrin was abolished by establishing covalent linkage of the protoporphyrin propionic acid side chains to fixed amines, demonstrating specific and directed binding: of rHA2 to these protoporphyrins. Amonoclonal antibody which recognizes a peptide epitope within the HA2 domain was employed to demonstrate that HA2-associated hemoglobin-binding activity was expressed and released by P. gingivalis cells in a batch culture, in parallel with proteinase activity. Cysteine proteinases from P. gingivalis appear to be multidomain proteins with functions for hemagglutination, erythrocyte lysis, proteolysis, and heme binding, as demonstrated here. Detailed understanding of the biochemical pathways for heme acquisition in P. gingivalis may allow precise targeting of this critical metabolic aspect for periodontal disease prevention.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 06:29:35