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Journal of Bacteriology, January 2009, p. 141-151, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.01221-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Pleiotropic Roles of Polyglycerolphosphate Synthase of Lipoteichoic Acid in Growth of Staphylococcus aureus Cells {triangledown} ,{dagger}

Yusuke Oku,1,{ddagger} Kenji Kurokawa,1,2* Miki Matsuo,1,§ Sakuo Yamada,3,4 Bok-Luel Lee,2 and Kazuhisa Sekimizu1

Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033,1 Department of Microbiology, Kawasaki Medical School, Matsushima 577, Kurashiki 701-0192,3 Department of Clinical Nutrition, Kawasaki University of Medical Welfare, Matsushima 288, Kurashiki 701-0193, Japan,4 National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University, Gumjeong-ku, Busan 609-735, South Korea2

Received 1 September 2008/ Accepted 14 October 2008

Lipoteichoic acid (LTA) is one of two anionic polymers on the surface of the gram-positive bacterium Staphylococcus aureus. LTA is critical for the bacterium-host cell interaction and has recently been shown to be required for cell growth and division. To determine additional biological roles of LTA, we found it necessary to identify permissive conditions for the growth of an LTA-deficient mutant. We found that an LTA-deficient S. aureus {Delta}ltaS mutant could grow at 30°C but not at 37°C. Even at the permissive temperature, {Delta}ltaS mutant cells had aberrant cell division and separation, decreased autolysis, and reduced levels of peptidoglycan hydrolases. Upshift of {Delta}ltaS mutant cells to a nonpermissive temperature caused an inability to exclude Sytox green dye. A high-osmolarity growth medium remarkably rescued the colony-forming ability of the {Delta}ltaS mutant at 37°C, indicating that LTA synthesis is required for growth under low-osmolarity conditions. In addition, the {Delta}ltaS mutation was found to be synthetically lethal with the {Delta}tagO mutation, which disrupts the synthesis of the other anionic polymer, wall teichoic acid (WTA), at 30°C, suggesting that LTA and WTA compensate for one another in an essential function.

* Corresponding author. Mailing address: Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Phone: 81-3-5841-4821. Fax: 81-3-5684-2973. E-mail: kurokawa{at}mol.f.u-tokyo.ac.jp

{triangledown} Published ahead of print on 24 October 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{ddagger} Present address: Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

§ Present address: Department of Bacteriology, Faculty of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.

Journal of Bacteriology, January 2009, p. 141-151, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.01221-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • 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]  


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