This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Mahapatra, S.
Right arrow Articles by Crick, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mahapatra, S.
Right arrow Articles by Crick, D. C.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2005, p. 2747-2757, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2747-2757.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mycobacterial Lipid II Is Composed of a Complex Mixture of Modified Muramyl and Peptide Moieties Linked to Decaprenyl Phosphate{dagger}

Sebabrata Mahapatra, Tetsuya Yagi,{ddagger} John T. Belisle, Benjamin J. Espinosa, Preston J. Hill, Michael R. McNeil, Patrick J. Brennan, and Dean C. Crick*

Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado

Received 8 November 2004/ Accepted 13 January 2005

Structural analysis of compounds identified as lipid I and II from Mycobacterium smegmatis demonstrated that the lipid moiety is decaprenyl phosphate; thus, M. smegmatis is the first bacterium reported to utilize a prenyl phosphate other than undecaprenyl phosphate as the lipid carrier involved in peptidoglycan synthesis. In addition, mass spectrometry showed that the muropeptides from lipid I are predominantly N-acetylmuramyl-L-alanine-D-glutamate-meso-diaminopimelic acid-D-alanyl-D-alanine, whereas those isolated from lipid II form an unexpectedly complex mixture in which the muramyl residue and the pentapeptide are modified singly and in combination. The muramyl residue is present as N-acetylmuramic acid, N-glycolylmuramic acid, and muramic acid. The carboxylic functions of the peptide side-chains of lipid II showed three types of modification, with the dominant one being amidation. The preferred site for amidation is the free carboxyl group of the meso-diaminopimelic acid residue. Diamidated species were also observed. The carboxylic function of the terminal D-alanine of some molecules is methylated, as are all three carboxylic acid functions of other molecules. This study represents the first structural analysis of mycobacterial lipid I and II and the first report of extensive modifications of these molecules. The observation that lipid I was unmodified strongly suggests that the lipid II intermediates of M. smegmatis are substrates for a variety of enzymes that introduce modifications to the sugar and amino acid residues prior to the synthesis of peptidoglycan.

* Corresponding author. Mailing address: Mycobacterial Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523. Phone: (970) 491-3308. Fax: (970) 491-1815. E-mail: Dean.Crick{at}colostate.edu.

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

{ddagger} Present address: Division of Respiratory Medicine, National Center for Geriatrics and Gerontology, Genko, Obu, Aichi, Japan.

Journal of Bacteriology, April 2005, p. 2747-2757, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2747-2757.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bhamidi, S., Scherman, M. S., Rithner, C. D., Prenni, J. E., Chatterjee, D., Khoo, K.-H., McNeil, M. R. (2008). The Identification and Location of Succinyl Residues and the Characterization of the Interior Arabinan Region Allow for a Model of the Complete Primary Structure of Mycobacterium tuberculosis Mycolyl Arabinogalactan. J. Biol. Chem. 283: 12992-13000 [Abstract] [Full Text]  
  • Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
  • Mahapatra, S., Crick, D. C., McNeil, M. R., Brennan, P. J. (2008). Unique Structural Features of the Peptidoglycan of Mycobacterium leprae. J. Bacteriol. 190: 655-661 [Abstract] [Full Text]  
  • Eoh, H., Brown, A. C., Buetow, L., Hunter, W. N., Parish, T., Kaur, D., Brennan, P. J., Crick, D. C. (2007). Characterization of the Mycobacterium tuberculosis 4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Synthase: Potential for Drug Development. J. Bacteriol. 189: 8922-8927 [Abstract] [Full Text]  
  • van Heijenoort, J. (2007). Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan. Microbiol. Mol. Biol. Rev. 71: 620-635 [Abstract] [Full Text]  
  • Berg, S., Kaur, D., Jackson, M., Brennan, P. J (2007). The glycosyltransferases of Mycobacterium tuberculosis--roles in the synthesis of arabinogalactan, lipoarabinomannan, and other glycoconjugates. Glycobiology 17: 35R-56R [Abstract] [Full Text]  
  • Dhiman, R. K., Schaeffer, M. L., Bailey, A. M., Testa, C. A., Scherman, H., Crick, D. C. (2005). 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase (IspC) from Mycobacterium tuberculosis: towards Understanding Mycobacterial Resistance to Fosmidomycin. J. Bacteriol. 187: 8395-8402 [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»