Outer Membrane Permeability of Pseudomonas aeruginosa

Nikaido, Hiroshi

doi:10.1016/b978-0-12-307210-8.50009-9

Cited by 70 publications

(79 citation statements)

References 157 publications

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“…aeruginosa, desferriferrioxamine B, desferriferrioxamine E, desferriferrichrysin and desferriferricrocin, generally had a substantially lower efficiency compared to the other siderophores and, interestingly, were totally inefficient when tested with the strain H636. This strain has an insertion in the gene for the outer-membrane protein OprF (Woodruff & Hancock, 1988), which has been shown to function as a porin, being a major uptake route across the outer membrane for hydrophilic compounds having a molecular mass less than 3000 Da (Nikaido & Hancock, 1986). This would suggest that ferrisiderophores may penetrate the bacterial cell through this pathway, and that the porin OprF is the only uptake route for iron complexes of desferriferrioxamine B, desferriferrioxamine E, desferriferrichrysin and desferriferricrocin.…”

Section: Discussionmentioning

confidence: 99%

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Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Meyer¹

1992

Journal of General Microbiology

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In addition to the two siderophores pyoverdine and pyochelin synthesized by Pseudomonas aeruginusu ATCC 15692 (strain PAOl), several siderophores produced by other bacteria or fungi, namely cepabactin, salicylic acid, desferriferrichrysin, desferriferricrocin, desferriferrioxamine B, desferriferrioxamine E and coprogen, were able to promote iron uptake with variable efficiencies into this bacterium. For most of these siderophores, these results were consistent with the growth stimulation produced by the same compounds in a plate bioassay. Desferriferriduome A, enterobactin and desferriferrirubin, however, did not promote iron uptake, although enterobactin and desferriferrirubin stimulated bacterial growth. These paradoxical data are discussed in view of siderophore-inducible iron uptake systems, as demonstrated recently for enterobactin. Among the strains tested, including the wild-type PAO1, the pyoverdine-less mutant PA06606 and the two porin-mutants P. ueruginusu H636 (oprl;: : a) and P. ueruginosu H673 (oprD: : Tn501), only for the porin-OprF mutant were fewer siderophores able to promote iron uptake compared to the other strains. Such results suggest that beside specific routes for iron uptake P. aerughsu is also able to take up siderophore-liganded iron through OprF.

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Section: Discussionmentioning

confidence: 99%

“…aeruginosa is described. In addition, the question of whether these siderophore-iron complexes utilize one of the known porin pathways, OprF (Nikaido & Hancock, 1986;Woodruff & Hancock, 1988) or OprD (Trias & Nikaido, 1990), as opposed to specific siderophore receptors, is explored.…”

Section: Introductionmentioning

confidence: 99%

Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Meyer¹

1992

Journal of General Microbiology

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“…Despite sharing rRNA homology, these two species have many differences including cell shape, optimal growth temperature, number of flagella, nutritional and metabolic properties, and guanosine plus cytosine (G+C) content of their DNA (67% for P. aeruginosa and 59 to 61% for P. syringae). Limited comparative studies on their outer membranes, however, have indicated some similarities (17, 19), although the outer membrane proteins of P. syringae, with the exception of the iron-regulated proteins (5), have received far less attention than have those of P. aeruginosa (17,26). In this study we examined in detail the well-characterized protein OprF and its structural gene to determine the extent of its conservation in the fluorescent pseudomonads and particularly in P. syringae.…”

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confidence: 99%

Conservation of the gene for outer membrane protein OprF in the family Pseudomonadaceae: sequence of the Pseudomonas syringae oprF gene

et al. 1991

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The conservation of the oprF gene for the major outer membrane protein OprF was determined by restriction mapping and Southern blot hybridization with the Pseudomonas aeruginosa oprF gene as a probe. The restriction map was highly conserved among 16 of the 17 serotype type strains and 42 clinical isolates of P. aeruginosa. Only the serotype 12 isolate and one clinical isolate showed small differences in restriction pattern. Southern probing of PstI chromosomal digests of 14 species from the family Pseudomonadaceae revealed that only the nine members of rRNA homology group I hybridized with the oprF gene. To reveal the actual extent of homology, the oprF gene and its product were characterized in Pseudomonas syringae. Nine strains of P. syringae from seven different pathovars hybridized with the P. aeruginosa gene to produce five different but related restriction maps. All produced an OprF protein in their outer membranes with the same apparent molecular weight as that of P. aeruginosa OprF. In each case the protein reacted with monoclonal antibody MA4-10 and was similarly heat and 2-mercaptoethanol modifiable. The purified OprF protein of the type strain P. syringae pv. syringae ATCC 19310 reconstituted small channels in lipid bilayer membranes. The oprF gene from this latter strain was cloned and sequenced. Despite the low level of DNA hybridization between P. aeruginosa and P. syringae DNA, the OprF gene was highly conserved between the species with 72% DNA sequence identity and 68% amino acid sequence identity overall. The carboxy terminus-encoding region of P. syringae oprF showed 85 and 33% identity, respectively, with the same regions of the P. aeruginosa oprF and Escherichia coli ompA genes.

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“…1). Moreover, the LPS core region of P. aeruginosa has been reported to have an unusually high phosphate content (35). Since cross-linking of phosphate groups by divalent cations is important for maintaining the integrity of the bacterial outer membrane, it is possible that the absence of heptose, and subsequently phosphate groups, may destabilize the membrane to the extent that the P. aeruginosa cells are no longer viable.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of two genes, waaC (rfaC) and waaF (rfaF), involved in Pseudomonas aeruginosa serotype O5 inner-core biosynthesis

Kievit

Lam

1997

J Bacteriol

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Recent studies have provided evidence to implicate involvement of the core oligosaccharide region of Pseudomonas aeruginosa lipopolysaccharide (LPS) in adherence to host tissues. To better understand the role played by LPS in the virulence of this organism, the aim of the present study was to clone and characterize genes involved in core biosynthesis. The inner-core regions of P. aeruginosa and Salmonella enterica serovar Typhimurium are structurally very similar; both contain two main chain residues of heptose linked to lipid A-Kdo 2 (Kdo is 3-deoxy-D-manno-octulosonic acid). By electrotransforming a P. aeruginosa PAO1 library into Salmonella waaC and waaF (formerly known as rfaC and rfaF, respectively) mutants, we were able to isolate the homologous heptosyltransferase I and II genes of P. aeruginosa. Two plasmids, pCOREc1 and pCOREc2, which restored smooth LPS production in the waaC mutant, were isolated. Similarly, plasmid pCOREf1 was able to complement the Salmonella waaF mutant. Sequence analysis of the DNA insert of pCOREc2 revealed one open reading frame (ORF) which could code for a protein of 39.8 kDa. The amino acid sequence of the deduced protein exhibited 53% identity with the sequence of the WaaC protein of S. enterica serovar Typhimurium. pCOREf1 contained one ORF capable of encoding a 38.4-kDa protein. The sequence of the predicted protein was 49% identical to the sequence of the Salmonella WaaF protein. Protein expression by the Maxicell system confirmed that a 40-kDa protein was encoded by pCOREc2 and a 38-kDa protein was encoded by pCOREf1. Pulsed-field gel electrophoresis was used to determine the map locations of the cloned waaC and waaF genes, which were found to lie between 0.9 and 6.6 min on the PAO1 chromosome. Using a gene-replacement strategy, we attempted to generate P. aeruginosa waaC and waaF null mutants. Despite multiple attempts to isolate true knockout mutants, all transconjugants were identified as merodiploids.Pseudomonas aeruginosa is an opportunistic pathogen capable of causing fatal infections in immunocompromised and debilitated individuals. The intrinsic resistance of this organism to many common antibiotics necessitates the development of new therapeutic strategies for treatment of infections. P. aeruginosa owes much of its success as a pathogen to its ability to elicit a wide variety of virulence determinants, including both secreted and cell-associated factors. Within this latter category is the amphipathic molecule lipopolysaccharide (LPS) (12). Most strains of P. aeruginosa coexpress two distinct forms of LPS known as A-band and B-band. A-band is an antigenically conserved molecule made up of D-rhamnose units (3), while B-band is the O-antigen-containing LPS. Chemical and structural differences in B-band LPS form the basis for dividing P. aeruginosa into the 20 serotypes recognized in the International Antigenic Typing Scheme (32, 33).The contribution of wild-type smooth LPS as an important virulence attribute of P. aeruginosa has been established in a number of studi...

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Outer Membrane Permeability of Pseudomonas aeruginosa

Cited by 70 publications

References 157 publications

Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Conservation of the gene for outer membrane protein OprF in the family Pseudomonadaceae: sequence of the Pseudomonas syringae oprF gene

Isolation and characterization of two genes, waaC (rfaC) and waaF (rfaF), involved in Pseudomonas aeruginosa serotype O5 inner-core biosynthesis

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