Disease relevance of Mirabilis

• A major peak with retention time of succinic acid was found in the broth cultures of all bacilli tested including H. influenzae, Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Proteus mirabilis, Citrobacter freundii, Pseudomonas aeruginosa, and Listeria monocytogenes [1].
• Infection caused by Proteus mirabilis strains with transferrable gentamicin-resistance factors [2].
• The fhaC gene product shows homology with ShIB and HpmB, two outer membrane proteins involved in export and activation of the haemolysins, ShIA and HpmA, of Serratia marcescens and Proteus mirabilis, respectively [3].
• In this study, the PAEs of ciprofloxacin against Pseudomonas aeruginosa, Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis, Serratia marcescens, Staphylococcus aureus, and Streptococcus faecalis were determined [4].
• 311, 99 and 59 pathogens were isolated from cefpodoxime proxetil, cefaclor and amoxicillin patients, respectively, the most common pathogens being Escherichia coli, Klebsiella spp., Proteus mirabilis, and Staphylococcus saprophyticus [5].

High impact information on Mirabilis

• Results of experiments in a laboratory model of a Foley catheterised bladder infected with P mirabilis showed that when retention balloons were inflated with a solution of triclosan (10 g/L), the catheters drained freely for at least 7 days [6].
• RESULTS: In the absence of urea, the acid tolerances of wild-type H. pylori, a urease-negative H. pylori mutant, Escherichia coli, and Proteus mirabilis were similar [7].
• During a period of 10 weeks, four patients in one hospital became infected with gentamicin-resistant Proteus mirabilis [2].
• Two extremely eurythermal goby fishes, Gillichthys mirabilis and Gillichthys seta, which encounter habitat temperature variations of approximately 30 degrees C, showed seasonal acclimatization of endogenous levels and of onset temperatures for enhanced synthesis of a 90-kDa-class heat shock protein (HSP90) [8].
• Tetradecapeptide somatostatin (10-80 microM) and its analog urotensin II (0.1-5 microM), a dodecapeptide from the urophysis of the teleost fish Gillichthys mirabilis, produced similar slowly developing relaxations of carbachol-induced tone [9].

Chemical compound and disease context of Mirabilis

• Lipopolysaccharide (LPS) isolated from Proteus mirabilis and administered to mice i.p. induced a primary immune response that consisted of the proliferation of only IgM antibody-producing cells [10].
• Cell differentiation of Proteus mirabilis is initiated by glutamine, a specific chemoattractant for swarming cells [11].
• Evidence that putrescine acts as an extracellular signal required for swarming in Proteus mirabilis [12].
• The outer membrane protein(s) of P. mirabilis and E. cloacae corresponding to E. coli porin were identified on the basis of their function, namely, their ability to allow the permeation of glucose as demonstrated by [14C]glucose uptake by intact cells [13].
• However, an unusually high rate of discrepancy was noted in several organism-antibiotic combinations, in particular E. coli and P. mirabilis with ampicillin, S. aureus with penicillin, and methicillin-resistant S. aureus with methicillin, erythromycin, and clindamycin [14].

Biological context of Mirabilis

• In vivo phase variation of MR/P fimbrial gene expression in Proteus mirabilis infecting the urinary tract [15].
• The results presented here suggest that the P. mirabilis and plasmid-encoded urease gene clusters utilize similar mechanisms of transcriptional activation in response to urea [16].
• Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme [17].
• Therefore, to study these problems, we constructed a fusion of ureA (a urease subunit gene) and lacZ (the beta-galactosidase gene) within plasmid pMID1010, which encodes an inducible urease of P. mirabilis expressed in E. coli JM103 (Lac-) [18].
• Alignment of the deduced amino acid sequence with those of known beta-lactamases revealed that CARB-5 possesses an RTG triad in box VII, as described for the Proteus mirabilis GN79 enzyme, instead of the RSG consensus characteristic of the other carbenicillinases [19].

Anatomical context of Mirabilis

• Flagella were markedly reduced as determined by scanning electron microscopy when P. mirabilis was grown in broth containing 20 mM salicylate [20].
• The role of the Fc and third component of complement (C3) receptors on mouse neutrophils in the control of killing of Proteus mirabilis, opsonized in normal mouse serum (NMS) or heated immune mouse serum (HIMS), was studied [21].
• In fatty tissues, concentrations were between 13 +/- 5 and 22 +/- 8 micrograms/g. All patients (15 of 15) had ceftriaxone levels in tissue greater than the MICs for the potential pathogens (Staphylococcus aureus, Escherichia coli, Klebsiella pneumoniae, and Proteus mirabilis) [22].
• Lipopolysaccharide from Proteus mirabilis O29 induces changes in red blood cell membrane lipids and proteins [23].
• Generation of hydrogen peroxide during the oxidation of L-phenylalanine by Proteus mirabilis isolated membranes [24].

Associations of Mirabilis with chemical compounds

• In striking contrast, the addition of 5 mmol/L of urea completely protected H. pylori but not P. mirabilis or C. jejuni from pH values as low as 1 [25].
• When cells of P. mirabilis containing NR1 are cultured in medium containing Cm at 250 microgram/ml a growth lag of 20-35 hr ensues [26].
• Gamma-irradiation induced high levels of nitrate reductase activity (NADH:nitrate oxidoreductase, EC 1.6.6.1) in callus of Haworthia mirabilis Haworth [27].
• Ribosome-inactivating and adenine polynucleotide glycosylase activities in Mirabilis jalapa L. tissues [28].
• The degradation was blocked by the metalloproteinase inhibitors GM6001 and 1, 10-phenantroline (both of which inhibited P. aeruginosa elastase, P. mirabilis proteinase, and E. faecalis gelatinase), or the inhibitor E64 (which inhibited S. pyogenes cysteine proteinase) [29].

Gene context of Mirabilis

• Cell invasion by P. mirabilis and mucin- and cell type-related distribution and response differences indicate bacterial tropism that affects crystal formation and mucosal presence [30].
• To explain different clinical significance of the strains we evaluated the biological activity of the lipopolysaccharides of P. mirabilis O3 and O18, as measured by interleukin-8 (IL-8) production [31].
• Ten clinical isolates of Proteus mirabilis were found to produce an inhibitor-resistant TEM beta-lactamase (IRT) in association with a TEM-1 enzyme [32].
• CONCLUSION: Our results suggest that antibodies against antigenic determinants of P. mirabilis in RA and K. pneumoniae in AS have cytotoxic properties on structurally related host proteins [33].
• Finally we have reconstituted recombination pathways of S marcescens and P mirabilis by combining the cloned recA and recBCD genes from these species in E coli deleted for recA and recBCD [34].

Analytical, diagnostic and therapeutic context of Mirabilis

• Proteus mirabilis is a common cause of urinary tract infection (UTI) in individuals with structural abnormalities or long-term catheterization [35].
• Crystallization of recA protein from Proteus mirabilis [36].
• An enzyme-linked immunosorbent assay using purified antigens showed a strong reaction between the MR/P fimbriae or flagella and sera of CBA mice challenged transurethrally with P. mirabilis [37].
• Against the Enterobacteriaceae (with the exception of Proteus mirabilis and Providencia stuartii) UK31214 and amikacin had similar degrees of activity (mode minimum inhibitory concentration [MIC], 1 microgram/ml) [38].
• With P. mirabilis, systemic immunization induced higher titers of specific serum agglutinins as compared with local respiratory tract immunization; however, local immunization was more effective in enhancing pulmonary bactericidal activity than was parenteral vaccination [39].

References