Disease relevance of Propionibacterium

• Using a murine granulomatous liver disease model induced by Propionibacterium acnes, we show that retention of Th1 cells in the LNs is controlled by a chemokine, CXCL10/interferon (IFN) inducible protein 10 produced by mature dendritic cells (DCs) [1].
• A blue bile pigment, possessing four acetic and four propionic acid side chains has been isolated from extracts of the anaerobic microorganism Clostridium tetanomorphum and in smaller amounts from Propionibacterium shermanii [2].
• The PMN cytotoxicities induced by the other immunomodulators, Propionibacterium acnes, Bacillus Calmette-Guérin, zymosan A, and Nocardia cell wall skeletons were also Ca2+ dependent, judging from studies with EGTA and measurement of hydrogen peroxide release in the presence and absence of Ca2+ [3].
• A calmodulin-dependent nitric oxide synthase was significantly induced in the liver of rats treated intravenously with heat-killed Propionibacterium acnes and 5 days later with Escherichia coli lipopolysaccharide [4].
• Blockade of secondary lymphoid tissue chemokine exacerbates Propionibacterium acnes-induced acute lung inflammation [5].

High impact information on Propionibacterium

• Interferon-gamma and IGIF were diminished in the sera of ICE-/- mice exposed to Propionibacterium acnes and lipopolysaccharide [6].
• In Propionibacterium acnes (P. acnes)-primed IL-18-deficient mice, LPS-induced IFNgamma production was markedly reduced, despite normal IL-12 induction [7].
• The capacity to inhibit CCR2 expression in monocytes was shared by other microbial agents and cytokines (inactivated Streptococci, Propionibacterium acnes, and to a lesser extent, IL-1 and TNF-alpha) [8].
• To establish the pathophysiological roles of TARC in vivo, we investigated whether a monoclonal antibody (mAb) against TARC could inhibit the induction of hepatic lesions in murine model using Propionibacterium acnes and lipopolysaccharide (LPS) [9].
• Peritoneal exudate cells (PEC) from Propionibacterium acnes-primed mice revealed increased glucose consumption during in vitro TNF production but showed no relationship between the degree of glucose consumption and the ability to produce TNF [10].

Chemical compound and disease context of Propionibacterium

• METHODS: We examined a functional role of inducible histamine in the protection against hepatic injury and lethality in Propionibacterium acnes -primed and lipopolysaccharide-induced hepatitis, using histidine decarboxylase knockout and H2-receptor knockout mice [11].
• Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and oxaloacetate [12].
• Transcarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and oxaloacetate [13].
• We have cloned the gene coding for the 1.3S biotin-containing subunit of transcarboxylase (EC 2.1.3.1) from Propionibacterium shermanii [14].
• On the basis of sequence homology with the Propionibacterium shermanii transcarboxylase 12S subunit, we suggest that the pccC domain, defined by Ile408 and Arg410, may involve the propionyl-CoA binding site [15].

Biological context of Propionibacterium

• The biotinated protein studied was the 1.3 S subunit of Propionibacterium shermanii, and transcarboxylase derepression was assayed by beta-galactosidase production in strains which carry a lacZ gene altered such that it is transcribed from biotin operon promoters [16].
• Both activities purified from Propionibacterium shermanii are the functional properties of a single enzyme with separate binding sites for the two phosphoryl donor substrates [17].
• Effects of diethylstilbestrol on Propionibacterium acnes immunomodulation: inhibition of macrophage activation and antitumor activity [18].
• IL-18 was cloned from a murine liver cell cDNA library generated from animals primed with heat-killed Propionibacterium acnes and subsequently challenged with lipopolysaccharide [(2) ] [19].
• When the biotin-accepting domain from the 1.3S subunit of Propionibacterium shermanii transcarboxylase (PSBT) is translationally fused to the periplasmic proteins alkaline phosphatase and maltose-binding protein, there is little or no biotinylation of PSBT in wild-type E. coli [20].

Anatomical context of Propionibacterium

• When a small amount of Gram-negative lipopolysaccharide was intravenously injected into mice which had been injected with heat-killed Propionibacterium acnes 7 days before, massive hepatic cell necrosis was induced and most of the mice died 24 hr later [21].
• An abnormality of the keratinizing epithelium of these follicles, thought to be due to the action of sebum synthesized and secreted by the androgen-sensitive sebaceous glands, leads to inflammation induced by the follicular bacterium, Propionibacterium acnes [22].
• Macrophages activated through treatment with Propionibacterium acnes ("Corynebacterium parvum"), on the other hand, did not bind free plasmodia in the presence of normal serum through systems inhibited by N-acetylmannosamine or N-acetylglucosamine [23].
• Various T-cell mitogens induced high levels of circulating gamma interferon (IFN-gamma) in mice that had been pretreated with Propionibacterium acnes [24].
• Prevention of endotoxin-induced acute lethality in Propionibacterium acnes-primed rabbits by an antibody to leukocyte integrin beta 2 with concomitant reduction of cytokine production [25].

Gene context of Propionibacterium

• To examine the role of IFN-gamma in lipopolysaccharide (LPS)-induced injury, we administered LPS (20 or 800 microg/mouse) alone or as low-dose LPS (20 microg/mouse) 7 days after heat-killed Propionibacterium acnes (P. acnes) injection into wild-type C57BL/6 (B6) mice or IFN-gamma-deficient (GKO) mice (B6 background) [26].
• We investigated the roles of TLR2 and TLR4 in Propionibacterium acnes (P. acnes)-primed, LPS-induced liver damage using selective TLR ligands [27].
• In acne, inflammation is due in part to the ability of Propionibacterium acnes to activate TLR2 [28].
• Requirement for TLR9 in the immunomodulatory activity of Propionibacterium acnes [29].
• In this study, we examined Propionibacterium acnes-primed TNF receptor p55-deficient (TNFRp55-/-) or Fas-deficient MRL/MpJ Lpr/Lpr mice challenged with lipopolysaccharide (LPS) [30].

Analytical, diagnostic and therapeutic context of Propionibacterium

• The same dose of Propionibacterium acnes and lipopolysaccharide induced severe hepatitis and high lethality in histidine decarboxylase knockout and H2-receptor knockout mice; the former were rescued by the subcutaneous injection of histamine [11].
• Expression of costimulatory molecules is significantly upregulated in various organs in an animal model of severe hepatitis induced by injection of Propionibacterium acnes (P. acnes) and lipopolysaccharide (LPS) [31].
• Crystallization and preliminary diffraction data for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii [32].
• Methylmalonyl-CoA mutase from Propionibacterium shermanii: characterization of the cobalamin-inhibited form and subunit-cofactor interactions studied by analytical ultracentrifugation [33].
• Inorganic pyrophosphate dependent D-fructose-6-phosphate 1-phosphotransferase from Propionibacterium freudenreichii was purified to apparent homogeneity by the criterion of silver staining on sodium dodecyl sulfate (SDS) gels [34].

References