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Journal of Bacteriology, April 2008, p. 2920-2932, Vol. 190, No. 8
0021-9193/08/$08.00+0     doi:10.1128/JB.01868-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification of a Second Lipopolysaccharide in Porphyromonas gingivalis W50{triangledown}

Minnie Rangarajan,1* Joseph Aduse-Opoku,1 Nikolay Paramonov,1 Ahmed Hashim,1 Nagihan Bostanci,2 Owen P. Fraser,3 Edward Tarelli,3 and Michael A. Curtis1

Centre for Infectious Disease, Institute of Cell and Molecular Science,1 Centre for Clinical and Diagnostic Oral Sciences, Barts and The London Queen Mary's School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom,2 Medical Biomics Centre, St. George's University of London, Cranmer Terrace, London SW17 0RE, United Kingdom3

Received 28 November 2007/ Accepted 28 January 2008

We previously described a cell surface anionic polysaccharide (APS) in Porphyromonas gingivalis that is required for cell integrity and serum resistance. APS is a phosphorylated branched mannan that shares a common epitope with posttranslational additions to some of the Arg-gingipains. This study aimed to determine the mechanism of anchoring of APS to the surface of P. gingivalis. APS was purified on concanavalin A affinity columns to minimize the loss of the anchoring system that occurred during chemical extraction. 1H nuclear magnetic resonance spectroscopy of the lectin-purified APS confirmed the previous structure but also revealed additional signals that suggested the presence of a lipid A. This was confirmed by fatty acid analysis of the APS and matrix-assisted laser desorption ionization-time of flight mass spectrometry of the lipid A released by treatment with sodium acetate buffer (pH 4.5). Hence, P. gingivalis synthesizes two distinct lipopolysaccharide (LPS) macromolecules containing different glycan repeating units: O-LPS (with O-antigen tetrasaccharide repeating units) and A-LPS (with APS repeating units). Nonphosphorylated penta-acylated and nonphosphorylated tetra-acylated species were detected in lipid A from P. gingivalis total LPS and in lipid A from A-LPS. These lipid A species were unique to lipid A derived from A-LPS. Biological assays demonstrated a reduced proinflammatory activity of A-LPS compared to that of total LPS. Inactivation of a putative O-antigen ligase (waaL) at PG1051, which is required for the final step of LPS biosynthesis, abolished the linkage of both the O antigen and APS to the lipid A core of O-LPS and A-LPS, respectively, suggesting that WaaL in P. gingivalis has dual specificity for both O-antigen and APS repeating units.

* Corresponding author. Mailing address: Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London Queen Mary's School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom. Phone: 0207 882 2320. Fax: 0207 882 2181. E-mail: m.rangarajan{at}qmul.ac.uk

{triangledown} Published ahead of print on 8 February 2008.

Journal of Bacteriology, April 2008, p. 2920-2932, Vol. 190, No. 8
0021-9193/08/$08.00+0     doi:10.1128/JB.01868-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Paramonov, N. A., Aduse-Opoku, J., Hashim, A., Rangarajan, M., Curtis, M. A. (2009). Structural Analysis of the Core Region of O-Lipopolysaccharide of Porphyromonas gingivalis from Mutants Defective in O-Antigen Ligase and O-Antigen Polymerase. J. Bacteriol. 191: 5272-5282 [Abstract] [Full Text]  
  • Sato, K., Kido, N., Murakami, Y., Hoover, C. I., Nakayama, K., Yoshimura, F. (2009). Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis. Microbiology 155: 1282-1293 [Abstract] [Full Text]  


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