Disease relevance of phoA

• Toxicity was significant including infections (20%), liver enzymes and alkaline phosphatase elevations (100%), and carmustine lung toxicity (7%) [1].
• Isolation and characterization of monoclonal antibodies against alkaline phosphatase of Pseudomonas aeruginosa [2].
• Serum concentrations of liver enzymes were significantly higher in infants with gram-negative bacteremia than in those with coagulase-negative staphylococcal bacteremia (P < 0.0001), but no difference in alkaline phosphatase serum values was observed [3].
• Intratracheal instillation of P. aeruginosa resulted in lung injury, as evidenced by increases in wet lung weight and decreases in the lung activities of angiotensin converting enzyme and alkaline phosphatase, enzymes localized primarily in pulmonary endothelial and alveolar type II epithelial cells, respectively [4].
• Biopsies of the proximal jejunal mucosa were taken through a jejunal fistula and the mucosal morphology and the activities of two brush border enzymes, lactase and alkaline phosphatase, were determined [5].

High impact information on phoA

• To verify the prediction, we analyzed the membrane topology of MexB using the alkaline phosphatase gene fusion method [6].
• The P. aeruginosa type II general secretory pathway (GSP) is used to export the largest number of proteins from this organism, including lipase, phospholipase C, alkaline phosphatase, exotoxin A, elastase and LasA [7].
• By sequential treatment with nucleotide pyrophosphatase and alkaline phosphatase, the flavin in each enzyme was shown to be in the dinucleotide form [8].
• No correlation occurred with peak serum level of antibiotic, creatinine, bilirubin, or alkaline phosphatase [9].
• Similarly, extraction of actively secreting cells with 0.2 M MgCl2 at pH 8.4 solubilized large quantities of the periplasmic enzyme alkaline phosphatase but insignificant amounts of phospholipase C. Bacteria continued to secrete enzyme for nearly 45 min after the addition of inorganic phosphate or rifampin [10].

Chemical compound and disease context of phoA

• The genes encoding the rrn operons, the 4.5S and 6S RNAs, elements of protein secretion, and outer membrane proteins F and I, and regulatory as well as structural genes for exotoxin A, alkaline phosphatase, and alginate and tryptophan biosynthesis, were assigned on the SpeI/DpnI macrorestriction map of the Pseudomonas aeruginosa PAO chromosome [11].
• Glutaraldehyde reactions with alkaline phosphatase of Pseudomonas aeruginosa [12].
• The existence of this activity which is induced jointly with phospholipase C by different choline metabolites, in a high phosphate medium, suggests that the attack of Pseudomonas aeruginosa on the cell host may also be produced under conditions of high phosphate concentrations, when the alkaline phosphatase is absent [13].
• In Pseudomonas aeruginosa, choline or betaine employed as the sole carbon and nitrogen source in a high phosphate medium induced a phospholipase C and an acid phosphatase activity but not an alkaline phosphatase activity [14].

Biological context of phoA

• The membrane topology of the hydrophobic domain was determined using the lacZ and phoA gene fusion approach [15].
• To investigate the topology of MexD more thoroughly, 25 MexD-PhoA (alkaline phosphatase) and 18 MexD-Bla (beta-lactamase) fusion plasmids were constructed and analyzed [16].
• Cell division in Pseudomonas aeruginosa: participation of alkaline phosphatase [17].
• We describe here a new mutant of Pseudomonas aeruginosa PAO, strain D10C (genotype plcB), which produces phospholipase C and alkaline phosphatase constitutively [18].
• In addition to LPS, several enzymes, such as phospholipase C, protease, hemolysin, and alkaline phosphatase, which are known to contribute to the pathogenicity of Pseudomonas infections were found to be present in both vesicle types [19].

Anatomical context of phoA

• By Western blotting and phoA fusion analyses, the MucB antagonist of sigma22 was found to localize to the periplasm of the cell [20].
• Diazo-7-amino-1,3-napthalenedisulfonic acid, a compound which does not penetrate the cytoplasmic membrane, completely inactivated rhodanese and alkaline phosphatase, a periplasmic enzyme, whereas lactic dehydrogenase retained its full activity [21].
• Ribonuclease and alkaline phosphatase are classed as enzymes which are readily extracted by osmotic shock and spheroplast formation whereas cyclic-2',3'-phosphodiesterase and 5'-nucleotidase are classed as enzymes which are not readily extracted by these procedures [22].

Associations of phoA with chemical compounds

• Data showing that a- and b-type flagellins gave positive immunoblots with antiphosphotyrosine monoclonal antibody and that release of P(i) by alkaline phosphatase occurred indicated that unmodified tyrosine phosphate exists in flagellin [23].
• Studies with media containing different levels of phosphate and with mutants of PAO1 suggested that protein P was coregulated with alkaline phosphatase and phospholipase C. Protein P was substantially purified and shown to form sodium dodecyl sulfate-resistant oligomers on polyacrylamide gels [24].
• In K. pneumoniae biofilms and colonies, alkaline phosphatase was initially expressed in the region of the biofilm immediately adjacent to the carbon and energy source (glucose) [25].
• These bilayered vesicles consist of endotoxin (lipopolysaccharide), outer membrane proteins and several potent hydrolytic enzymes including protease, alkaline phosphatase, phospholipase C and peptidoglycan hydrolase [26].
• Comparative studies on the inactivation of alkaline phosphatase by glutaraldehyde showed significant differences when the purified protein was compared with whole, cell-bound enzyme [12].

Other interactions of phoA

• Using a mexA-phoA fusion, expression of the efflux genes was assessed as a function of growth in a variety of strains [27].
• We show that PilD, encoding a putative pilin-specific leader peptidase, also controls export of alkaline phosphatase, phospholipase C, elastase, and exotoxin A. pilD mutants accumulate these proteins in the periplasmic space, while secretion of periplasmic and outer membrane proteins appears to be normal [28].

Analytical, diagnostic and therapeutic context of phoA

• Measurements with an oxygen microelectrode indicated that oxygen was depleted locally within the biofilm and that the oxygen-replete zone was of a dimension similar to that of the biologically active zone, as indicated by alkaline phosphatase induction [29].
• Sequence analysis and complementation studies showed that the P. aeruginosa phoU gene was involved both in the regulation of AP expression and in the induction of P(i) taxis [30].

References