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 Turner, M. S.
Right arrow Articles by Giffard, P. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Turner, M. S.
Right arrow Articles by Giffard, P. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 1999, p. 2192-2198, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The bspA Locus of Lactobacillus fermentum BR11 Encodes an L-Cystine Uptake System

Mark S. Turner,1 Tonia Woodberry,2 Louise M. Hafner,1 and Philip M. Giffard1,*

Centre for Molecular Biotechnology, School of Life Sciences, Queensland University of Technology,1 and Queensland Institute of Medical Research, Herston,2 Brisbane, Australia

Received 14 September 1998/Accepted 26 January 1999

BspA is a basic surface-exposed protein from Lactobacillus fermentum BR11. Sequence comparisons have shown that it is a member of family III of the solute binding proteins. It is 89% identical to the collagen binding protein, Cnb, from Lactobacillus reuteri. Compared with the database of Escherichia coli proteins, BspA is most similar to the L-cystine binding protein FliY. To investigate the function of BspA, mutants depleted for BspA were generated by homologous recombination with a temperature-sensitive plasmid. These mutants were significantly impaired in their abilities to take up L-cystine. Uptake rates of L-glutamine, L-histidine, and L-lysine, which are substrates for other binding proteins with similarity to BspA, were unaffected. Evidence was obtained that BspA is necessary for maximal resistance to oxidative stress. Specifically, inactivation of BspA causes defective growth in the presence of oxygen and sensitivity to paraquat. Measurements of sulfhydryl levels showed that incubation of L. fermentum BR11 with L-cystine resulted in increased levels of sulfhydryl groups both inside and outside the cell; however, this was not the case with a BspA mutant. The role of BspA as an extracellular matrix protein adhesin was also addressed. L. fermentum BR11 does not bind to immobilized type I collagen or laminin above background levels but does bind immobilized fibronectin. Inactivation of BspA did not significantly affect fibronectin binding; therefore, we have not found evidence to support the notion that BspA is an extracellular matrix protein binding adhesin. As BspA is most probably not a lipoprotein, this report provides evidence that gram-positive bacterial solute binding proteins do not necessarily have to be anchored to the cytoplasmic membrane to function in solute uptake.

* Corresponding author. Mailing address: Centre for Molecular Biotechnology, School of Life Sciences, Queensland University of Technology, G.P.O. Box 2434, Brisbane, Queensland 4001, Australia. Phone: (61-7) 3864-2015. Fax: (61-7) 3864-1534. E-mail: p.giffard{at}qut.edu.au.

Journal of Bacteriology, April 1999, p. 2192-2198, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Lo, R., Turner, M. S., Barry, D. G., Sreekumar, R., Walsh, T. P., Giffard, P. M. (2009). Cystathionine {gamma}-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11. J. Bacteriol. 191: 1827-1837 [Abstract] [Full Text]  
  • Jansch, A., Korakli, M., Vogel, R. F., Ganzle, M. G. (2007). Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451T: Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs. Appl. Environ. Microbiol. 73: 4469-4476 [Abstract] [Full Text]  
  • Turner, M. S., Lo, R., Giffard, P. M. (2007). Inhibition of Staphylococcus aureus Growth on Tellurite-Containing Media by Lactobacillus reuteri Is Dependent on CyuC and Thiol Production. Appl. Environ. Microbiol. 73: 1005-1009 [Abstract] [Full Text]  
  • Bruno-Barcena, J. M., Andrus, J. M., Libby, S. L., Klaenhammer, T. R., Hassan, H. M. (2004). Expression of a Heterologous Manganese Superoxide Dismutase Gene in Intestinal Lactobacilli Provides Protection against Hydrogen Peroxide Toxicity. Appl. Environ. Microbiol. 70: 4702-4710 [Abstract] [Full Text]  
  • Burguiere, P., Auger, S., Hullo, M.-F., Danchin, A., Martin-Verstraete, I. (2004). Three Different Systems Participate in L-Cystine Uptake in Bacillus subtilis. J. Bacteriol. 186: 4875-4884 [Abstract] [Full Text]  
  • Turner, M. S., Hafner, L. M., Walsh, T., Giffard, P. M. (2004). Identification and Characterization of the Novel LysM Domain-Containing Surface Protein Sep from Lactobacillus fermentum BR11 and Its Use as a Peptide Fusion Partner in Lactobacillus and Lactococcus. Appl. Environ. Microbiol. 70: 3673-3680 [Abstract] [Full Text]  
  • Turner, M. S., Hafner, L. M., Walsh, T., Giffard, P. M. (2003). Peptide Surface Display and Secretion Using Two LPXTG-Containing Surface Proteins from Lactobacillus fermentum BR11. Appl. Environ. Microbiol. 69: 5855-5863 [Abstract] [Full Text]  
  • Boles, B. R., McCarter, L. L. (2002). Vibrio parahaemolyticus scrABC, a Novel Operon Affecting Swarming and Capsular Polysaccharide Regulation. J. Bacteriol. 184: 5946-5954 [Abstract] [Full Text]  
  • Sutcliffe, I. C., Harrington, D. J. (2002). Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148: 2065-2077 [Abstract] [Full Text]  
  • Turner, M. S., Giffard, P. M. (1999). Expression of Chlamydia psittaci- and Human Immunodeficiency Virus-Derived Antigens on the Cell Surface of Lactobacillus fermentum BR11 as Fusions to BspA. Infect. Immun. 67: 5486-5489 [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»