IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Kim, J. H.
Right arrow Articles by Nahm, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, J. H.
Right arrow Articles by Nahm, M. H.
Infection and Immunity, February 2005, p. 834-840, Vol. 73, No. 2
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.2.834-840.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Monoacyl Lipoteichoic Acid from Pneumococci Stimulates Human Cells but Not Mouse Cells

Je Hak Kim,1 Hoseong Seo,1,2 Seung Hyun Han,1,3 Jisheng Lin,1 Moon-Kook Park,4 Uffe B. S. Sorensen,5 and Moon H. Nahm1,2*

Department of Pathology,1 Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama,2 Faculty of Biological Sciences, Chonbuk National University, Jeonju,4 International Vaccine Institute, Seoul, South Korea,3 Institute of Medical Microbiology and Immunology, University of Aarhus, Aarhus, Denmark5

Received 12 August 2004/ Returned for modification 28 September 2004/ Accepted 6 October 2004

We have developed a method for obtaining pneumococcal lipoteichoic acid (LTA) with none, one, or two acyl chains. Anion-exchange chromatography at pH 9.5 yields pneumococcal LTA (labeled LTA-9.5) that has a mass spectrum identical to that of pre-ion-exchange LTA and loses 500 mass units after deacylation by alkali hydrolysis. Anion exchange at pH 10.5 produces LTA (labeled LTA-10.5) with mass peaks that are 264 mass units lower than those of pre-ion-exchange LTA, and deacylation of LTA-10.5 by alkali hydrolysis reduces the mass by only 239 mass units. This result indicates that LTA-10.5 has lost one of the two acyl chains, whereas LTA-9.5 has both acyl chains. When the biological properties of LTA-9.5 and LTA-10.5 are examined with mouse cells, only LTA-9.5 (and not LTA-10.5) is able to stimulate mouse cells to produce tumor necrosis factor alpha, interleukin-1ß, and nitric oxide. In contrast, both LTA-9.5 and LTA-10.5 can stimulate human cells. LTA became inactive when both acyl chains were removed. Thus, acyl chains are critical for LTA function, and small variations in acyl chains can alter biological properties of LTA.

* Corresponding author. Mailing address: Department of Pathology, UAB, 845 19th St., South (BBRB-614), Birmingham, AL 35294. Phone: (205) 934-0163. Fax: (205) 975-2149. E-mail: nahm{at}UAB.edu.

Editor: A. D. O'Brien

Infection and Immunity, February 2005, p. 834-840, Vol. 73, No. 2
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.2.834-840.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.