This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Higa, F.
Right arrow Articles by Edelstein, P. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Higa, F.
Right arrow Articles by Edelstein, P. H.

 Previous Article  |  Next Article 

Infection and Immunity, August 2001, p. 4782-4789, Vol. 69, No. 8
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.8.4782-4789.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Potential Virulence Role of the Legionella pneumophila ptsP Ortholog

Futoshi Higa1,2 and Paul H. Edelstein1,3,*

Department of Pathology and Laboratory Medicine1 and Department of Medicine,3 University of Pennsylvania Medical School, Philadelphia, PA 19104-4283, and First Department of Internal Medicine, Faculty of Medicine, University of the Ryukyus, Okinawa 903-0215, Japan2

Received 26 October 2000/Returned for modification 5 February 2001/Accepted 2 May 2001

We previously identified the Legionella pneumophila ptsP (phosphoenolpyruvate phosphotransferase) ortholog gene as a putative virulence factor in a study of signature-tagged mutagenesis using a guinea pig pneumonia model. In this study, we further defined the phenotypic properties of L. pneumophila ptsP and its complete sequence. The L. pneumophila ptsP was 2,295 bases in length. Its deduced amino acid sequence had high similarity with ptsP orthologs of Pseudomonas aeruginosa, Azotobacter vinelandii, and Escherichia coli, with nearly identical lengths. Here we show that while the mutant grew well in laboratory media, it was defective in both lung and spleen multiplication in guinea pigs. It grew slowly in guinea pig alveolar macrophages despite good uptake into the cells. Furthermore, there was minimal growth in a human alveolar epithelial cell line (A549). Transcomplementation of the L. pneumophila ptsP mutant almost completely rescued its growth in alveolar macrophages, in A549 cells, and in guinea pig lung and spleen. The L. pneumophila ptsP mutant was capable of evasion of phagosome-lysosome fusion and resided in ribosome-studded phagosomes. Pore formation activity of the mutant was normal. The L. pneumophila ptsP mutant expressed DotA and IcmX in apparently normal amounts, suggesting that the ptsP mutation did not affect dotA and icmX regulation. In addition, the mutant was resistant to serum and neutrophil killing. Taken together, these findings show that L. pneumophila ptsP is required for full in vivo virulence of L. pneumophila, most probably by affecting intracellular growth.

* Corresponding author. Mailing address: Clinical Microbiology Laboratory, 4 Gates, Department of Pathology and Laboratory Medicine, Hospital of the University of Pennsylvania, 3400 Spruce St., Philadelphia, PA 19104-4283. Phone: (215) 662-6651. Fax: (215) 662-6655. E-mail: phe{at}mail.med.upenn.edu.

Infection and Immunity, August 2001, p. 4782-4789, Vol. 69, No. 8
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.8.4782-4789.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Aurass, P., Pless, B., Rydzewski, K., Holland, G., Bannert, N., Flieger, A. (2009). bdhA-patD Operon as a Virulence Determinant, Revealed by a Novel Large-Scale Approach for Identification of Legionella pneumophila Mutants Defective for Amoeba Infection. Appl. Environ. Microbiol. 75: 4506-4515 [Abstract] [Full Text]  
  • Velazquez, F., Pfluger, K., Cases, I., De Eugenio, L. I., de Lorenzo, V. (2007). The Phosphotransferase System Formed by PtsP, PtsO, and PtsN Proteins Controls Production of Polyhydroxyalkanoates in Pseudomonas putida. J. Bacteriol. 189: 4529-4533 [Abstract] [Full Text]  
  • Deutscher, J., Francke, C., Postma, P. W. (2006). How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria. Microbiol. Mol. Biol. Rev. 70: 939-1031 [Abstract] [Full Text]  
  • Mavrodi, O. V., Mavrodi, D. V., Weller, D. M., Thomashow, L. S. (2006). Role of ptsP, orfT, and sss Recombinase Genes in Root Colonization by Pseudomonas fluorescens Q8r1-96. Appl. Environ. Microbiol. 72: 7111-7122 [Abstract] [Full Text]  
  • Higa, F., Akamine, M., Haranaga, S., Tohyama, M., Shinzato, T., Tateyama, M., Koide, M., Saito, A., Fujita, J. (2005). In vitro activity of pazufloxacin, tosufloxacin and other quinolones against Legionella species. J Antimicrob Chemother 56: 1053-1057 [Abstract] [Full Text]  
  • Miyake, M., Watanabe, T., Koike, H., Molmeret, M., Imai, Y., Abu Kwaik, Y. (2005). Characterization of Legionella pneumophila pmiA, a Gene Essential for Infectivity of Protozoa and Macrophages. Infect. Immun. 73: 6272-6282 [Abstract] [Full Text]  
  • Edelstein, P. H., Hu, B., Shinzato, T., Edelstein, M. A. C., Xu, W., Bessman, M. J. (2005). Legionella pneumophila NudA Is a Nudix Hydrolase and Virulence Factor. Infect. Immun. 73: 6567-6576 [Abstract] [Full Text]  
  • Ismail, T. M., Hart, C. A., McLennan, A. G. (2003). Regulation of Dinucleoside Polyphosphate Pools by the YgdP and ApaH Hydrolases Is Essential for the Ability of Salmonella enterica serovar Typhimurium to Invade Cultured Mammalian Cells. J. Biol. Chem. 278: 32602-32607 [Abstract] [Full Text]  
  • Edelstein, P. H., Hu, B., Higa, F., Edelstein, M. A. C. (2003). lvgA, a Novel Legionella pneumophila Virulence Factor. Infect. Immun. 71: 2394-2403 [Abstract] [Full Text]  
  • Ewann, F., Jackson, M., Pethe, K., Cooper, A., Mielcarek, N., Ensergueix, D., Gicquel, B., Locht, C., Supply, P. (2002). Transient Requirement of the PrrA-PrrB Two-Component System for Early Intracellular Multiplication of Mycobacterium tuberculosis. Infect. Immun. 70: 2256-2263 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»