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Altered expression of oligopeptide-binding protein (OppA) and aminoglycoside resistance in laboratory and clinical Escherichia coli strains

Laboratório de Genética de Microrganismos, Departamento de Microbiologia, ICB, Universidade de São Paulo, São Paulo, 05508-900, SP and *Laboratório de Fisiologia Celular, Instituto de Biofísica Carlos Chagas Filho, CCS, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21949-900, RJ, Brazil

Corresponding author Dr S. O. P. Costa (e-mail: sopdcost@ icb.usp.br).

Received 5 May 1999; revised edition received 20 Sept. 1999; accepted 21 Sept. 1999.

Abstract

Oligopeptide-binding protein (OppA) is the periplasmic component of the major oligopeptide transport system of enteric bacteria. Genetic and biochemical evidence suggests that OppA plays a role in the uptake of aminoglycoside antibiotics in Escherichia coli K-12. Forty-six (82%) of 56 aminoglycoside-resistant mutants of E. coli K-12 selected in vitro had reduced or undetectable OppA levels, as compared with their parent strain. Moreover, nine (36%) of 25 aminoglycoside-resistant clinical isolates of E. coli expressed reduced or undetectable levels of OppA. No decrease in OppA expression was observed among aminoglycoside-sensitive E. coli strains from patients. Twenty-three (42%) of 56 aminoglycoside-resistant mutants of E. coli K-12 and six (24%) of 25 clinical isolates also were deficient for expression of ornithine or arginine decarboxylases, or both, and these deficiencies might negatively affect OppA expression by reducing polyamine synthesis. These results support the view that reduced OppA expression is associated with aminoglycoside resistance in E. coli strains.

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