Abstract
The outer membrane permeability of Serratia marcescens was studied by comparing porin-deficient mutants with their parental strains. Omp1-deficient strains were selected by moxalactam resistance, whereas mutants lacking the Omp2 porin were obtained by experimental infection with the SMP2 phage, whose primary receptor is the Omp2 porin. The role of porins was demonstrated in quinolone accumulation assays, where semiquantitative differences in accumulation were observed. Permeability coefficients to cephaloridine of Omp1 mutants were determined and compared with those of the parental strain. The clinical isolates S. marcescens HCPR1 and 866 showed 30- to 200-fold reduced permeability coefficients when Omp1 porin was absent.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology*
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Anti-Infective Agents / metabolism
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Bacterial Outer Membrane Proteins / metabolism
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Bacterial Outer Membrane Proteins / physiology
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Bacteriophages / drug effects
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Bacteriophages / genetics
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Bacteriophages / ultrastructure
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Ciprofloxacin / metabolism
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Culture Media
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Drug Resistance, Bacterial
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Electrophoresis, Polyacrylamide Gel
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Extracellular Matrix Proteins / physiology
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Fish Proteins*
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Kinetics
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Microbial Sensitivity Tests
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Mutation
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Permeability
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Porins / genetics
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Porins / physiology*
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Serratia marcescens / drug effects*
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Serratia marcescens / genetics
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Serratia marcescens / metabolism
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beta-Lactamases / metabolism
Substances
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Anti-Bacterial Agents
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Anti-Infective Agents
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Bacterial Outer Membrane Proteins
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Culture Media
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Extracellular Matrix Proteins
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Fish Proteins
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Omp2 protein, bacteria
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Porins
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Ciprofloxacin
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beta-Lactamases