Disease relevance of ORF184

• Pseudomonas aeruginosa porin OprF: properties of the channel [1].
• Earlier studies have shown that the major porin species in Pseudomonas aeruginosa outer membrane is protein F (OprF), which produces channels wider than those produced by Escherichia coli porins [2].
• The susceptibility of beta-lactamase-producing strains and known porin mutants of the Enterobacteriaceae suggests that CGP 31608 is resistant to many important beta-lactamases (including the mutationally derepressed chromosomal enzymes) and is not excluded from the bacterial cell in strains expressing these known porin mutations [3].
• By using purified preparations of Salmonella typhimurium and Pseudomonas aeruginosa porins, in the presence of polymyxin B, it was possible to induce concentration-dependent loss of calcium from cultured murine calvaria at porin concentrations in the range of 1 to 10 nM [4].
• In contrast, porin-induced bone resorption could be inhibited by relatively high concentrations of the natural inhibitor of interleukin-1 (IL-1 receptor antagonist) [4].

High impact information on ORF184

• Western blot analysis revealed reduced expression of the basic amino acid and carbapenem-specific OprD porin in all imipenem-resistant mutants [5].
• The role of specific lysine residues in the passage of anions through the Pseudomonas aeruginosa porin OprP [6].
• Cloning and nucleotide sequence of anaerobically induced porin protein E1 (OprE) of Pseudomonas aeruginosa PAO1 [7].
• Comparison of the derived amino acid sequence with the known sequences of other bacterial porins demonstrated that OprP could be no better aligned to these porin sequences than it could to the periplasmic phosphate-binding protein PhoS of Escherichia coli [8].
• C-terminal region of Pseudomonas aeruginosa outer membrane porin OprD modulates susceptibility to meropenem [9].

Chemical compound and disease context of ORF184

• Mutational loss of the D2 porin causes imipenem resistance in Pseudomonas aeruginosa [10].
• Distribution of porin and lipopolysaccharide antigens on a Pseudomonas aeruginosa permeability mutant [11].
• Salicylate, a weak aromatic acid known to reduce porin expression and induce low levels of multiple antibiotic resistance in Escherichia coli, was able to induce imipenem resistance and reduce the expression of OprD but not multiple antibiotic resistance or OprN expression in P. aeruginosa [12].
• We found by proteoliposome swelling assays that cefepime, cefpirome, and E-1040 all penetrated the porin channels of Escherichia coli and E. cloacae much more rapidly than did ceftazidime and at least as rapidly as did cefotaxime [13].
• Outer membrane protein F (porin) was purified by extraction from polyacrylamide gels of cell envelope proteins of the Pseudomonas aeruginosa PAO1 strain [14].

Biological context of ORF184

• Osmotic stress, salicylate, and Mar (multiple antibiotic resistance) mutation are known to block the expression of the OmpF porin [15].
• A number of carbapenem derivatives were examined to determine the structure-activity relationships required for dependence on porin protein D2 for activity against Pseudomonas aeruginosa [16].
• Phagocytosis of in vivo-grown P. aeruginosa cells could be further enhanced by using a porin protein F-specific monoclonal antibody [17].
• In conclusion, BO-2727 exhibited improved activity against imipenem-resistant P. aeruginosa, probably because of its ability to overcome loss of the D2 porin and beta-lactamase hydrolysis [18].
• Insertion mutagenesis of the Pseudomonas aeruginosa phosphate-specific porin OprP [19].

Anatomical context of ORF184

• Similar channel sizes were observed for porin protein F purified by the same method from P. aeruginosa outer membranes [20].

Associations of ORF184 with chemical compounds

• These results suggested that in Mueller-Hinton medium the uptake of BMY 45047 through the non-D2 pathway is more rapid than that of meropenem through the D2 porin [16].
• No aminoglycoside-modifying enzymes were observed, and outer membrane compositional analyses of the resistant variants revealed porin protein and lipopolysaccharide profiles similar to those of the aminoglycoside-susceptible parental strain (PA-96) [21].
• Salicylate had no apparent effect, however, on expression of a 40-kDa porin protein in P. mirabilis [15].
• This suggests that OprH is not a porin but, instead, may cause increased uptake of quinolones and chloramphenicol via a non-porin pathway [22].
• Conversely, binding of [14C]imipenem in a porin D2-positive strain was reduced by sparfloxacin but not by the nonamphoteric quinolone nalidixic acid [23].

Analytical, diagnostic and therapeutic context of ORF184

• Membrane topology and site-specific mutagenesis of Pseudomonas aeruginosa porin OprD [24].
• Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF [25].
• OprB, a glucose-inducible porin of P. aeruginosa, was characterized by black lipid bilayer analysis and circular dichroism spectroscopy [26].
• The resultant porin preparations were found to be devoid of detectable lipopolysaccharide (LPS) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining for LPS, direct enzyme-linked immunosorbent assays with LPS-specific monoclonal antibodies, and 2-keto-3-deoxyoctulosonic acid assays [27].
• Determination of the minimum inhibitory concentrations of beta-lactams, fluoroquinolones, chloramphenicol and gentamicin in these mutants revealed that most mutants showed equal susceptibility to the porin-sufficient strain [28].

References