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 Gründling, A.
Right arrow Articles by Schneewind, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gründling, A.
Right arrow Articles by Schneewind, O.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2007, p. 2521-2530, Vol. 189, No. 6
0021-9193/07/$08.00+0     doi:10.1128/JB.01683-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Genes Required for Glycolipid Synthesis and Lipoteichoic Acid Anchoring in Staphylococcus aureus{triangledown}

Angelika Gründling and Olaf Schneewind*

Department of Microbiology, University of Chicago, Chicago, Illinois 60637

Received 31 October 2006/ Accepted 26 December 2006

Staphylococcus aureus lipoteichoic acid (LTA) is composed of a linear 1,3-linked polyglycerolphosphate chain and is tethered to the bacterial membrane by a glycolipid (diglucosyl-diacylglycerol [Glc2-DAG]). Glc2-DAG is synthesized in the bacterial cytoplasm by YpfP, a processive enzyme that transfers glucose to diacylglycerol (DAG), using UDP-glucose as its substrate. Here we present evidence that the S. aureus {alpha}-phosphoglucomutase (PgcA) and UTP:{alpha}-glucose 1-phosphate uridyltransferase (GtaB) homologs are required for the synthesis of Glc2-DAG. LtaA (lipoteichoic acid protein A), a predicted membrane permease whose structural gene is located in an operon with ypfP, is not involved in Glc2-DAG synthesis but is required for synthesis of glycolipid-anchored LTA. Our data suggest a model in which LtaA facilitates the transport of Glc2-DAG from the inner (cytoplasmic) leaflet to the outer leaflet of the plasma membrane, delivering Glc2-DAG as a substrate for LTA synthesis, thereby generating glycolipid-anchored LTA. Glycolipid anchoring of LTA appears to play an important role during infection, as S. aureus variants lacking ltaA display defects in the pathogenesis of animal infections.

* Corresponding author. Mailing address: Department of Microbiology, 920 East 58th Street, Chicago, IL 60637. Phone: (773) 843-9060. Fax: (773) 834-8150. E-mail: oschnee{at}bsd.uchicago.edu.

{triangledown} Published ahead of print on 5 January 2007.

Journal of Bacteriology, March 2007, p. 2521-2530, Vol. 189, No. 6
0021-9193/07/$08.00+0     doi:10.1128/JB.01683-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Thammavongsa, V., Kern, J. W., Missiakas, D. M., Schneewind, O. (2009). Staphylococcus aureus synthesizes adenosine to escape host immune responses. JEM 206: 2417-2427 [Abstract] [Full Text]  
  • Sava, I. G., Zhang, F., Toma, I., Theilacker, C., Li, B., Baumert, T. F., Holst, O., Linhardt, R. J., Huebner, J. (2009). Novel Interactions of Glycosaminoglycans and Bacterial Glycolipids Mediate Binding of Enterococci to Human Cells. J. Biol. Chem. 284: 18194-18201 [Abstract] [Full Text]  
  • Kurokawa, K., Lee, H., Roh, K.-B., Asanuma, M., Kim, Y. S., Nakayama, H., Shiratsuchi, A., Choi, Y., Takeuchi, O., Kang, H. J., Dohmae, N., Nakanishi, Y., Akira, S., Sekimizu, K., Lee, B. L. (2009). The Triacylated ATP Binding Cluster Transporter Substrate-binding Lipoprotein of Staphylococcus aureus Functions as a Native Ligand for Toll-like Receptor 2. J. Biol. Chem. 284: 8406-8411 [Abstract] [Full Text]  
  • Lu, D., Wormann, M. E., Zhang, X., Schneewind, O., Grundling, A., Freemont, P. S. (2009). Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS. Proc. Natl. Acad. Sci. USA 106: 1584-1589 [Abstract] [Full Text]  
  • Seo, H. S., Cartee, R. T., Pritchard, D. G., Nahm, M. H. (2008). A New Model of Pneumococcal Lipoteichoic Acid Structure Resolves Biochemical, Biosynthetic, and Serologic Inconsistencies of the Current Model. J. Bacteriol. 190: 2379-2387 [Abstract] [Full Text]  
  • Grundling, A., Schneewind, O. (2007). Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 104: 8478-8483 [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»