This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tinsley, C. R. Articles by Gotschlich, E. C. Search for Related Content PubMed PubMed Citation Articles by Tinsley, C. R. Articles by Gotschlich, E. C.

 Previous Article  |  Next Article 

Infect. Immun., May 1995, 1624-1630, Vol 63, No. 5
Copyright © 1995, American Society for Microbiology

Cloning and characterization of the meningococcal polyphosphate kinase gene: production of polyphosphate synthesis mutants

CR Tinsley and EC Gotschlich
Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021-6399, USA.

The pathogenic Neisseria species accumulate polyphosphate to levels between 10 and 20% of their total phosphate content. However, the significance of this compound for the growth and pathogenicity of these species is not understood. A previous report (C.R. Tinsley, B.N. Manjula, and E.C. Gotschlich, Infect. Immun. 61:3703-3710, 1993) describes the purification of polyphosphate kinase, the enzyme responsible for synthesis of polyphosphate, from Neisseria meningitidis BNCV. By use of probes based on the amino acid sequence of the purified enzyme, the structural gene ppk has been cloned and sequenced. The coding sequence is 2,055 bp long and codes for a protein of 77.2 kDa. The open reading frame of the cloned gene was interrupted by the insertion of a kanamycin resistance cassette, and ppk mutants were obtained in both Neisseria gonorrhoeae and N. meningitidis by transformation with the recombinant plasmid. Amounts of polyphosphate in the ppk mutants were reduced to between 2 and 10% of wild-type levels. The mutants grew less vigorously than wild-type organisms in vitro and showed a striking increase in sensitivity to killing by human serum.

This article has been cited by other articles:

• Candon, H. L., Allan, B. J., Fraley, C. D., Gaynor, E. C. (2007). Polyphosphate Kinase 1 Is a Pathogenesis Determinant in Campylobacter jejuni. J. Bacteriol. 189: 8099-8108 [Abstract] [Full Text]  
• Tobin, K. M., McGrath, J. W., Mullan, A., Quinn, J. P., O'Connor, K. E. (2007). Polyphosphate Accumulation by Pseudomonas putida CA-3 and Other Medium-Chain-Length Polyhydroxyalkanoate-Accumulating Bacteria under Aerobic Growth Conditions. Appl. Environ. Microbiol. 73: 1383-1387 [Abstract] [Full Text]  
• Boyce, K. J., Kretschmer, M., Kronstad, J. W. (2006). The vtc4 Gene Influences Polyphosphate Storage, Morphogenesis, and Virulence in the Maize Pathogen Ustilago maydis.. Eukaryot Cell 5: 1399-1409 [Abstract] [Full Text]  
• Brown, M. R. W., Kornberg, A. (2004). Inorganic polyphosphate in the origin and survival of species. Proc. Natl. Acad. Sci. USA 101: 16085-16087 [Abstract] [Full Text]  
• Ayraud, S., Janvier, B., Salaun, L., Fauchere, J.-L. (2003). Modification in the ppk Gene of Helicobacterpylori during Single and Multiple Experimental Murine Infections. Infect. Immun. 71: 1733-1739 [Abstract] [Full Text]  
• Ishige, K., Zhang, H., Kornberg, A. (2002). Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP. Proc. Natl. Acad. Sci. USA 99: 16684-16688 [Abstract] [Full Text]  
• McMahon, K. D., Dojka, M. A., Pace, N. R., Jenkins, D., Keasling, J. D. (2002). Polyphosphate Kinase from Activated Sludge Performing Enhanced Biological Phosphorus Removal. Appl. Environ. Microbiol. 68: 4971-4978 [Abstract] [Full Text]  
• Chen, W., Palmer, R. J., Kuramitsu, H. K. (2002). Role of Polyphosphate Kinase in Biofilm Formation by Porphyromonas gingivalis. Infect. Immun. 70: 4708-4715 [Abstract] [Full Text]  
• Kim, K.-S., Rao, N. N., Fraley, C. D., Kornberg, A. (2002). Inorganic polyphosphate is essential for long-term survival and virulence factors in Shigella and Salmonella spp.. Proc. Natl. Acad. Sci. USA 99: 7675-7680 [Abstract] [Full Text]  
• Snyder, L. A. S., Butcher, S. A., Saunders, N. J. (2001). Comparative whole-genome analyses reveal over 100 putative phase-variable genes in the pathogenic Neisseria spp.. Microbiology 147: 2321-2332 [Abstract] [Full Text]  
• Ishige, K., Noguchi, T. (2000). Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proc. Natl. Acad. Sci. USA 10.1073/pnas.011518098v1 [Abstract] [Full Text]  
• McGrath, J. W., Quinn, J. P. (2000). Intracellular Accumulation of Polyphosphate by the Yeast Candida humicola G-1 in Response to Acid pH. Appl. Environ. Microbiol. 66: 4068-4073 [Abstract] [Full Text]  
• Klee, S. R., Nassif, X., Kusecek, B., Merker, P., Beretti, J.-L., Achtman, M., Tinsley, C. R. (2000). Molecular and Biological Analysis of Eight Genetic Islands That Distinguish Neisseria meningitidis from the Closely Related Pathogen Neisseria gonorrhoeae. Infect. Immun. 68: 2082-2095 [Abstract] [Full Text]  
• NGHIÊM, H.-O., BETTENDORFF, L., CHANGEUX, J.-P. (2000). Specific phosphorylation of Torpedo 43K rapsyn by endogenous kinase(s) with thiamine triphosphate as the phosphate donor. FASEB J. 14: 543-554 [Abstract] [Full Text]  
• Tzeng, C.-M., Kornberg, A. (2000). The Multiple Activities of Polyphosphate Kinase of Escherichia coli and Their Subunit Structure Determined by Radiation Target Analysis. J. Biol. Chem. 275: 3977-3983 [Abstract] [Full Text]  
• Rashid, M. H., Rao, N. N., Kornberg, A. (2000). Inorganic Polyphosphate Is Required for Motility of Bacterial Pathogens. J. Bacteriol. 182: 225-227 [Abstract] [Full Text]  
• Kumble, K. D., Ahn, K., Kornberg, A. (1996). Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli. Proc. Natl. Acad. Sci. USA 93: 14391-14395 [Abstract] [Full Text]  
• Ishige, K., Noguchi, T. (2000). Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proc. Natl. Acad. Sci. USA 97: 14168-14171 [Abstract] [Full Text]