The role of OmpC and OmpF in acidic resistance in Escherichia coli

Biol Pharm Bull. 2011;34(3):330-4. doi: 10.1248/bpb.34.330.

Abstract

The roles of OmpC and OmpF in acidic resistance (AR) were examined. When ompC and ompF were deleted, AR was decreased. The decreased level of AR seen in the mutant that was deficient in ompC and ompF was elevated by the addition of glutamate, but not by the addition of arginine or lysine. The expression levels of adiA and cadB were diminished by the deletion of ompC and ompF, and the conversion of arginine to agmatine and lysine to cadaverine by intact cells were reduced in the mutant. The expression of gadA/gadB was not affected by the deletion of ompC and ompF. These results suggest that the transport of arginine, lysine, and their decarboxylated products through OmpC and/or OmpF is essential for the survival of Escherichia coli cells under extremely acidic conditions.

MeSH terms

  • Acids
  • Amino Acid Transport Systems / genetics
  • Amino Acid Transport Systems / metabolism
  • Amino Acids / metabolism*
  • Antiporters / genetics
  • Antiporters / metabolism
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Biological Transport
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli / pathogenicity
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Glutamate Decarboxylase / genetics
  • Glutamate Decarboxylase / metabolism
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mutation
  • Porins / genetics
  • Porins / metabolism*
  • Stress, Physiological / genetics*

Substances

  • Acids
  • Amino Acid Transport Systems
  • Amino Acids
  • Antiporters
  • Bacterial Outer Membrane Proteins
  • CadB protein, E Coli
  • Escherichia coli Proteins
  • Membrane Proteins
  • Porins
  • Carboxy-Lyases
  • gadA protein, E coli
  • Glutamate Decarboxylase
  • arginine decarboxylase