Intrinsic antibiotic resistance of <i>Pseudomonas aeruginosa</i>

Hancock, Robert E. W.

doi:10.1093/jac/18.6.653

Cited by 49 publications

(21 citation statements)

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“…Several of the other OM proteins were reduced in all three adapted strains. However, since the aminoglycoside antibiotics are believed not to use OM porins for entry but to cross the OM by a self-promoted pathway involving binding to cationic binding sites within the OM (Abdel-Sayed et al, 1982;Hancock, 1986), the possible significance of the reduced content of these OM proteins is uncertain. However, the reduction in several bands in the 73-69-Kda range is noteworthy since Morris and Brown (1988) recently reported that subinhibitory concentrations of the aminoglycosides inhibit the production of iron-chelating siderophores.…”

Section: Discussionmentioning

confidence: 99%

“…It has been proposed (Hancock, 1981(Hancock, , 1986Abdel-Sayed et al, 1982;Eagon, 1984;Taber et al, 1987) that the aminoglycoside antibiotics penetrate through the OM via a self-promoted pathway mediated by binding to cation-binding sites within the OM. Both the polymyxins and the aminoglycosides are thought to bind to the same sites within the OM, and Hancock and co-workers (Nicas andHancock, 1980, 1983;Hancock, 1981;Hancock et al, 1981) have proposed that induction of OM-protein H1 in P. aeruginosa confers resistance to both the polymyxins and the aminoglycosides by protecting the binding site on LPS from attack.…”

Section: Introductionmentioning

confidence: 99%

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Adaptive resistance to aminoglycoside antibiotics in Pseudomonas aeruginosa

Gilleland

Gibson

et al. 1989

Journal of Medical Microbiology

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Summary. Aminoglycoside-resistant variants of Pseudornonas aeruginosa strain P A 0 1 were readily selected by culturing the organism in medium containing increasing concentrations of gentamicin, tobramycin or amikacin until the strains were growing in a concentration of drug 128-fold greater than the minimal inhibitory concentration for the sensitive parent strain. These resistant strains exhibited characteristics previously associated with the impermeability type of resistance mechanism, i.e., they grew more slowly than the parent strain, the resistance was unstable in the absence of the antibiotic, and adaptation to one of the antibiotics conferred crossresistance to other aminoglycosides. The adapted strains grew, with minimal morphological alterations, in concentrations of the various aminoglycosides that normally produced cell envelope damage, misshapen and filamentous cell formation, and cell lysis in the sensitive strain. Neither protein H1 nor phospholipid alterations appear to play a significant role in adaptive resistance to aminoglycoside antibiotics in this model system. The acquisition of adaptive resistance to the aminoglycoside antibiotics did not confer resistance to polymyxin B, another cationic antibiotic which is thought to share binding sites within the outer membrane with the aminoglycosides.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Adaptive resistance to aminoglycoside antibiotics in Pseudomonas aeruginosa

Gilleland

Gibson

et al. 1989

Journal of Medical Microbiology

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“…Treatment of P. aeruginosa infections is hindered by the high intrinsic resistance of this pathogen to many commonly used antibiotics (21). For patients with an intact defense system, active immunization against P. aeruginosa could prevent infections.…”

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confidence: 99%

Sequence and transcriptional start site of the Pseudomonas aeruginosa outer membrane porin protein F gene

et al. 1988

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Porin F is one of the major proteins of the outer membrane of Pseudomonas aeruginosa. It forms water-filled pores of variable size. Porin F is a candidate for a vaccine against P. aeruginosa because it antigenically cross-reacts in all serotype strains of the International Antigenic Typing Scheme. We have isolated the gene for porin F from a lambda EMBL3 bacteriophage library by using oligodeoxynucleotide hybridization probes and have determined its nucleotide sequence. Different peptide sequences obtained from isolated porin F confirmed the deduced protein sequence. The mature protein consists of 326 amino acid residues and has a molecular weight of 35,250. The precursor contains an N-terminal signal peptide of 24 amino acid residues. S1 protection and primer extension experiments, together with Northern (RNA) blots, indicate that the mRNA coding for porin F is monocistronic with short untranslated regions of about 58 bases at the 5' end and about 47 bases at the 3' end. The sequences in the -10 and -35 regions upstream of the transcriptional start site are closely related to the Escherichia coli promoter consensus sequences, which explains why the porin F gene is expressed in E. coli under the control of its own promoter. The amino acid sequence of porin F is not homologous to the different E. coli porins OmpF, OmpC, LamB, and PhoE. On the other hand, a highly homologous region of 30 amino acids between the OmpA proteins of different enteric bacteria and porin F of P. aeruginosa was detected. The core region of the homology to E. coli OmpA had 11 of 12 amino acid residues in common.

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“…Pseudomonads cause infections, e.g., in immunocompromised patients, that are difficult to treat. The high natural resistance of these pathogens against ,-lactams is based on their low outer membrane permeability (5,7,11,13,15; R. G. Hewinson, M. P. E. Slack, and W. W. Nichols, in J. Ishigami, ed., Recent Advances in Chemotherapy, Proc. 14th Int.…”

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confidence: 99%

Physiological studies of the regulation of beta-lactamase expression in Pseudomonas maltophilia

Rosta

Mett

1989

J Bacteriol

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The kinetics of j-lactamase induction in Pseudomonas maltophilia 1ID1275/873 were investigated. Upon induction with ,3-lactam antibiotics, a correlation was seen between the increase in specific P-lactamase activity and the generation time, as well as the concentration of inducer in the medium. The specific P-lactamase activity increased slowly within the first 0.5 generation and then more rapidly; it decreased regularly after about 2 generations of growth in the presence of inducer. This decrease could presumably be attributed to the continuous breakdown of inducer by ,-lactamases in the culture medium. In a chemostat culture with continuous supply of fresh inducer-containing medium, the specific 13-lactamase activity could be stabilized at a high level over several generations. Removal of the 13-lactam after a certain induction time showed that a short exposure of the bacteria to inducer caused induction kinetics comparable to those resulting from continuous exposure of the cells to inducer. The two P-lactamases of P. maltophilia, L1 and L2, were induced simultaneously under various experimental conditions. Pseudomonads cause infections, e.g., in immunocompromised patients, that are difficult to treat. The high natural resistance of these pathogens against ,-lactams is based on their low outer membrane permeability (5, 7, 11, 13, 15; R. G. Hewinson, M. P.

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Intrinsic antibiotic resistance of Pseudomonas aeruginosa

Cited by 49 publications

References 0 publications

Adaptive resistance to aminoglycoside antibiotics in Pseudomonas aeruginosa

Adaptive resistance to aminoglycoside antibiotics in Pseudomonas aeruginosa

Sequence and transcriptional start site of the Pseudomonas aeruginosa outer membrane porin protein F gene

Physiological studies of the regulation of beta-lactamase expression in Pseudomonas maltophilia

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