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 Zbell, A. L.
Right arrow Articles by Maier, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zbell, A. L.
Right arrow Articles by Maier, R. J.

 Previous Article  |  Next Article 

Infection and Immunity, October 2008, p. 4445-4454, Vol. 76, No. 10
0019-9567/08/$08.00+0     doi:10.1128/IAI.00741-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Salmonella enterica Serovar Typhimurium NiFe Uptake-Type Hydrogenases Are Differentially Expressed In Vivo {triangledown}

Andrea L. Zbell, Susan E. Maier, and Robert J. Maier*

Department of Microbiology, University of Georgia, Athens, Georgia

Received 11 June 2008/ Returned for modification 27 June 2008/ Accepted 5 July 2008

Salmonella enterica serovar Typhimurium, a common enteric pathogen, possesses three NiFe uptake-type hydrogenases. The results from mouse infection studies suggest that the H2 oxidation capacity provided by these hydrogenases is important for virulence. Since the three enzymes are similar in structure and function, it may be expected that they are utilized under different locations and times during an infection. A recombination-based method to examine promoter activity in vivo (RIVET) was used to determine hydrogenase gene expression in macrophages, polymorphonuclear leukocyte (PMN)-like cells, and a mouse model of salmonellosis. The hyd and hya promoters showed increased expression in both murine macrophages and human PMN-like cells compared to that in the medium-only controls. Quantitative reverse transcription-PCR results suggested that hyb is also expressed in phagocytes. A nonpolar hya mutant was compromised for survival in macrophages compared to the wild type. This may be due to lower tolerance to acid stress, since the hya mutant was much more acid sensitive than the wild type. In addition, hya mutant cells were internalized by macrophages the same as wild-type cells. Mouse studies (RIVET) indicate that hyd is highly expressed in the liver and spleen early during infection but is expressed poorly in the ileum in infected animals. Late in the infection, the hyd genes were expressed at high levels in the ileum as well as in the liver and spleen. The hya genes were expressed at low levels in all locations tested. These results suggest that the hydrogenases are used to oxidize hydrogen in different stages of an infection.


* Corresponding author. Mailing address: Department of Microbiology, 527 Biological Sciences Building, University of Georgia, Athens, GA 30602. Phone: (706) 542-2323. Fax: (706) 542-2674. E-mail: rmaier{at}uga.edu

{triangledown} Published ahead of print on 14 July 2008.

Editor: A. J. Bäumler


Infection and Immunity, October 2008, p. 4445-4454, Vol. 76, No. 10
0019-9567/08/$08.00+0     doi:10.1128/IAI.00741-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Zbell, A. L., Maier, R. J. (2009). Role of the Hya Hydrogenase in Recycling of Anaerobically Produced H2 in Salmonella enterica Serovar Typhimurium. Appl. Environ. Microbiol. 75: 1456-1459 [Abstract] [Full Text]