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 Brubaker, R. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brubaker, R. R.

 Previous Article  |  Next Article 

Infection and Immunity, August 2005, p. 4743-4752, Vol. 73, No. 8
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.8.4743-4752.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Influence of Na+, Dicarboxylic Amino Acids, and pH in Modulating the Low-Calcium Response of Yersinia pestis

Robert R. Brubaker*

Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan 48824

Received 10 January 2005/ Returned for modification 4 March 2005/ Accepted 11 April 2005

The virulence of yersiniae is promoted in part by shared {approx}70-kb plasmids (pCD in Yersinia pestis and pYV in enteropathogenic Yersinia pseudotuberculosis and Yersinia enterocolitica) that mediate a low-calcium response. This phenotype is characterized at 37°C by either bacteriostasis in Ca2+-deficient medium with expression of pCD/pYV-encoded virulence effectors (Yops and LcrV) or vegetative growth and repression of Yops and LcrV with ≥2.5 mM Ca2+ (Lcr+). Regulation of Yops and LcrV is well defined but little is known about bacteriostasis other than that Na+ plus L-glutamate promotes prompt restriction of Y. pestis. As shown here, L-aspartate substituted for L-glutamate in this context but only Na+ exacerbated the nutritional requirement for Ca2+. Bacteriostasis of Y. pestis (but not enteropathogenic yersiniae) was abrupt in Ca2+-deficient medium at neutral to slightly alkaline pH (7.0 to 8.0), although increasing the pH to 8.5 or 9.0, especially with added Na+ (but not L-glutamate), facilitated full-scale growth. Added L-glutamate (but not Na+) favored Ca2+-independent growth at acidic pH (5.0 to 6.5). Yops and LcrV were produced in Ca2+-deficient media at pH 6.5 to 9.0 regardless of the presence of added Na+ or L-glutamate, although their expression at alkaline pH was minimal. Resting Ca2+-starved Lcr+ cells of Y. pestis supplied with L-glutamate first excreted and then destroyed L-aspartate. These findings indicate that expression of Yops and LcrV is necessary but not sufficient for bacteriostasis of Ca2+-starved yersiniae and suggest that abrupt restriction of Y. pestis requires Na+ and the known absence of aspartate ammonia-lyase in this species.

* Mailing address: Department of Microbiology and Molecular Genetics, 2209 Biophysical Medical Sciences Building, Michigan State University, East Lansing, MI 48824. Phone: (517) 355-6463, ext. 1576. Fax: (517) 353-8957. E-mail: brubake3{at}msu.edu.

Editor: V. J. DiRita

Infection and Immunity, August 2005, p. 4743-4752, Vol. 73, No. 8
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.8.4743-4752.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhou, D., Yang, R. (2009). Molecular Darwinian Evolution of Virulence in Yersinia pestis. Infect. Immun. 77: 2242-2250 [Full Text]  
  • Schmid, A., Neumayer, W., Trulzsch, K., Israel, L., Imhof, A., Roessle, M., Sauer, G., Richter, S., Lauw, S., Eylert, E., Eisenreich, W., Heesemann, J., Wilharm, G. (2009). Cross-talk between Type Three Secretion System and Metabolism in Yersinia. J. Biol. Chem. 284: 12165-12177 [Abstract] [Full Text]  
  • Bearden, S. W., Sexton, C., Pare, J., Fowler, J. M., Arvidson, C. G., Yerman, L., Viola, R. E., Brubaker, R. R. (2009). Attenuated enzootic (pestoides) isolates of Yersinia pestis express active aspartase. Microbiology 155: 198-209 [Abstract] [Full Text]  
  • Viola, R. E., Yerman, L., Fowler, J. M., Arvidson, C. G., Brubaker, R. R. (2008). A missense mutation causes aspartase deficiency in Yersinia pestis. Microbiology 154: 1271-1280 [Abstract] [Full Text]  
  • Myers-Morales, T., Cowan, C., Gray, M. E., Wulff, C. R., Parker, C. E., Borchers, C. H., Straley, S. C. (2007). A Surface-Focused Biotinylation Procedure Identifies the Yersinia pestis Catalase KatY as a Membrane-Associated but Non-Surface-Located Protein. Appl. Environ. Microbiol. 73: 5750-5759 [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»