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Journal of Bacteriology, March 2008, p. 1783-1791, Vol. 190, No. 5
0021-9193/08/$08.00+0     doi:10.1128/JB.01046-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Function of a Mycobacterial Major Facilitator Superfamily Pump Requires a Membrane-Associated Lipoprotein{triangledown}

Mary F. Farrow1,2 and Eric J. Rubin1,2*

Department of Immunology and Infectious Diseases, Harvard School of Public Health,1 Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 021152

Received 3 July 2007/ Accepted 14 December 2007

The lprG-Rv1410c operon is critical for the survival of Mycobacterium tuberculosis during infection, but very little is known about the functions of its proteins. LprG is a lipoprotein, and Rv1410c encodes the major facilitator superfamily small molecule transporter P55. P55 likely exports small molecules outside of the bacterial cell, but the function of LprG is unclear. A deletion of the homologous operon in Mycobacterium smegmatis is more susceptible to ethidium bromide, and drug resistance is restored by the intact operon from M. tuberculosis. The multidrug resistance pump inhibitor reserpine inhibits resistance to ethidium bromide in both wild-type M. smegmatis and the complemented mutant, suggesting that P55-mediated transport is responsible for drug resistance and that ethidium bromide is a novel substrate for P55. In addition to hypersensitivity to ethidium bromide, cells that lack the lprG-Rv1410c operon display abnormal colony morphology and are defective for sliding motility, properties that suggest an alteration of cell wall composition. Strikingly, both ethidium bromide transport and normal cell surface properties require functional P55 and LprG, as neither alone is sufficient to restore function to the deletion mutant. Thus, P55 requires the cell surface lipoprotein for normal function.

* Corresponding author. Mailing address: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115. Phone: (617) 432-3335. Fax: (617) 432-3259. E-mail: erubin{at}hsph.harvard.edu

{triangledown} Published ahead of print on 21 December 2007.

Journal of Bacteriology, March 2008, p. 1783-1791, Vol. 190, No. 5
0021-9193/08/$08.00+0     doi:10.1128/JB.01046-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ramon-Garcia, S., Martin, C., Thompson, C. J., Ainsa, J. A. (2009). Role of the Mycobacterium tuberculosis P55 Efflux Pump in Intrinsic Drug Resistance, Oxidative Stress Responses, and Growth. Antimicrob. Agents Chemother. 53: 3675-3682 [Abstract] [Full Text]  
  • Stewart, C. R., Rossier, O., Cianciotto, N. P. (2009). Surface Translocation by Legionella pneumophila: a Form of Sliding Motility That Is Dependent upon Type II Protein Secretion. J. Bacteriol. 191: 1537-1546 [Abstract] [Full Text]  
  • Danilchanka, O., Mailaender, C., Niederweis, M. (2008). Identification of a Novel Multidrug Efflux Pump of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 52: 2503-2511 [Abstract] [Full Text]  


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