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Clinical and Vaccine Immunology, April 2006, p. 452-458, Vol. 13, No. 4
1071-412X/06/$08.00+0     doi:10.1128/CVI.13.4.452-458.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Platelet-Activating Factor-Acetylhydrolase Can Monodeacylate and Inactivate Lipoteichoic Acid

Ho Seong Seo,2 Je Hak Kim,1 and Moon H. Nahm1,2*

Departments of Pathology,1 Microbiology, University of Alabama at Birmingham, Birmingham, Alabama2

Received 29 September 2005/ Returned for modification 8 December 2005/ Accepted 18 January 2006

Bacterial lipoteichoic acid (LTA) shares a structural motif with platelet-activating factor (PAF). Both molecules are strong inflammatory agents and have a glycerol backbone with two lipid chains at the sn-1 and sn-2 positions. PAF is normally inactivated by PAF-acetylhydrolase (PAF-AH), a phospholipase A2 (PLA2), which removes a short acyl group at the sn-2 position. To investigate whether PAF-AH can similarly degrade LTA, we studied the effects of porcine PLA2, bee venom PLA2, and recombinant human PAF-AH on pneumococcal LTA (PnLTA) and staphylococcal LTA (StLTA). After incubation with a porcine or bee venom PLA2, a large fraction of PnLTA lost 264 Da, which corresponds to the mass of the oleic acid group at the sn-2 position. After incubation with recombinant human PAF-AH, PnLTA lost 264 Da; the reduction did not occur when PAF-AH was exposed to Pefabloc SC, an irreversible inhibitor of the PAF-AH active site. Following PAF-AH treatment, PnLTA and StLTA were not able to stimulate mouse RAW 264.7 cells to produce tumor necrosis factor alpha but could stimulate CHO cells expressing human TLR2. This stimulation pattern has been observed with monoacyl PnLTA prepared by mild alkali hydrolysis (22). Taking these data together, we conclude that PAF-AH can remove one acyl chain at the sn-2 position of LTA and produce a monoacyl-LTA that is inactive against mouse cells.

* Corresponding author. Mailing address: Department of Pathology, University of Alabama at Birmingham, 845 19th St. South (BBRB 614), Birmingham, AL 35249-7331. Phone: (205) 934-0163. Fax: (205) 975-2149. E-mail: Nahm{at}uab.edu.

Clinical and Vaccine Immunology, April 2006, p. 452-458, Vol. 13, No. 4
1071-412X/06/$08.00+0     doi:10.1128/CVI.13.4.452-458.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Seo, H. S., Michalek, S. M., Nahm, M. H. (2008). Lipoteichoic Acid Is Important in Innate Immune Responses to Gram-Positive Bacteria. Infect. Immun. 76: 206-213 [Abstract] [Full Text]  


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