Disease relevance of tpr

• Expression of the tpr protease gene of Porphyromonas gingivalis is regulated by peptide nutrients [1].
• In an Escherichia coli background, tpr transcription was initiated after an AT-rich region upstream of tpr but not at the P. gingivalis start site [1].
• Purification and characterization of a thiol-protease from Bacteroides gingivalis strain 381 [2].

High impact information on tpr

• However, inactivation of the major rgpA gene resulted in increased transcription of the prtT and tpr protease genes while decreasing expression of the Lys-gingipain kgp gene as detected by Northern blot analysis [3].
• In the present study, we further characterized expression of the tpr gene using a tpr::lacZ reporter gene construct under a range of nutrient conditions [1].
• Deletion mutations in the tpr upstream region identified the promoter region immediately upstream of the transcription start site, determined by primer extension analysis [1].
• Three identical 17-bp direct repeats identified within the 5' end of tpr mRNA were involved in tpr regulation [1].
• An isogenic mutant lacking a functional tpr gene had a greatly reduced ability to hydrolyze the collagenase substrate [4].

Chemical compound and disease context of tpr

• From the culture supernatant of Bacteroides gingivalis ATCC 33277, a thiol protease was purified to homogeneity by fractional ammonium sulfate precipitation, ion-exchange chromatography, gel filtration, and isoelectric focusing [5].

Biological context of tpr

• Activity was restored to the tpr mutant by introducing a shuttle plasmid containing the tpr gene [4].

Anatomical context of tpr

• The ability of P. gingivalis to attach to erythrocytes and epithelial cells was found to be affected by the presence of arginine and thiol protease inhibitors (leupeptin, p-chloromercuriphenylsulfonic acid) [6].

Associations of tpr with chemical compounds

• B. gingivalis possesses cell-associated fibrinogenolytic activity that is activated by dithiothreitol and blocked by thiol protease inhibitors [7].
• Analysis of this prtR gene revealed that the predicted nascent product contains a protease domain followed by a haemagglutinin domain and is post-translationally processed by proteolytic (possibly autolytic) events to produce a 43-54 kDa arginine-specific, thiol protease and a 41-53 kDa haemagglutinin [8].

Analytical, diagnostic and therapeutic context of tpr

• Immunoblotting analysis of these enzymes using a polyclonal antibody against Pase-S, which is a soluble, clostripain-like protease, revealed immunological distinction from Pase-C, a vesicle-associated thiol-protease [9].

References