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Infection and Immunity, December 2000, p. 7069-7077, Vol. 68, No. 12
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
OppA of Listeria monocytogenes, an
Oligopeptide-Binding Protein Required for Bacterial Growth at Low
Temperature and Involved in Intracellular Survival
Elise
Borezee,
Elisabeth
Pellegrini, and
Patrick
Berche*
Inserm U411, Faculté de Médecine Necker, 75730 Paris Cedex 15, France
Received 19 July 2000/Returned for modification 17 August
2000/Accepted 6 September 2000
We identified a new oligopeptide permease operon in the pathogen
Listeria monocytogenes. This opp operon
consists of five genes (oppA, oppB, oppC, oppD, and
oppF) and displays the same genetic organization as those
of several bacterial species. The first gene of this operon,
oppA, encodes a 62-kDa protein sharing 33% identity with
OppA of Bacillus subtilis and is expressed predominantly during exponential growth. The function of oppA was studied
by constructing an oppA deletion mutant. The phenotype
analysis of this mutant revealed that OppA mediates the transport of
oligopeptides and is required for bacterial growth at low temperature.
The wild-type phenotype was restored by complementing the mutant with
oppA. We also found that OppA is involved in intracellular
survival in macrophages and in bacterial growth in organs of mice
infected with L. monocytogenes, although the level of
virulence was not altered in the mutant. These results show the major
role of OppA in the uptake of oligopeptides and the pleiotropic effects
of this oligopeptide-binding protein on the behavior of this pathogen in the environment and in its host.
*
Corresponding author. Mailing address: INSERM U411,
Faculté de Médecine Necker, 156, rue de Vaugirard, 75730 Paris
Cedex 15, France. Phone: [33] 1 40 61 53 71. Fax: [33] 1 40 61 55 92. E-mail: berche{at}necker.fr.
Infection and Immunity, December 2000, p. 7069-7077, Vol. 68, No. 12
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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