This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schwebach, J. R. Articles by Casadevall, A. Search for Related Content PubMed PubMed Citation Articles by Schwebach, J. R. Articles by Casadevall, A.

 Previous Article  |  Next Article 

Infection and Immunity, May 2002, p. 2566-2575, Vol. 70, No. 5
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.5.2566-2575.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Glucan Is a Component of the Mycobacterium tuberculosis Surface That Is Expressed In Vitro and In Vivo

Department of Microbiology and Immunology,¹ Department of Pediatrics, Children's Hospital at Montefiore,² Analytical Imaging Facility,³ Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461,⁴ National Institute of Child Health and Human Development Biotechnology Unit, National Institutes of Health, Bethesda, Maryland 20892⁵

Received 18 July 2001/ Returned for modification 8 October 2001/ Accepted 16 January 2002

The outermost layer of Mycobacterium tuberculosis is composed primarily of two polysaccharides, glucan (GC) and arabinomannan. To analyze the surface polysaccharide composition of M. tuberculosis, we generated a monoclonal antibody (MAb) that binds M. tuberculosis GC and is known as MAb 24c5. Immunofluorescence and whole-mount immunoelectron microscopy indicated that GC is on the outermost portion of the bacteria. M. tuberculosis strains Erdman and CDC 1551 were analyzed for their ability to bind MAb 24c5 after in vitro growth in media with and without the detergent Tween 80. MAb 24c5 bound to Erdman and CDC 1551 at all culture times with only slightly greater apparent affinity after extended culture in the absence of Tween 80, indicating that a stable amount of GC polysaccharide antigen is associated with the cell surface of M. tuberculosis. An enzyme-linked immunosorbent assay indicated that GC is antigenically similar to glycogen, and the amount of GC antigen increased in the media of M. tuberculosis cultures grown either with or without the detergent Tween 80. Other nontuberculosis mycobacteria have antigenically similar GCs on their surfaces after in vitro growth. Inoculation of mice with live bacilli but not inoculation with dead bacilli elicited a strong antibody response to GC consistent with production of this antigen in vivo. Our results provide a more comprehensive picture of the M. tuberculosis cell envelope and the conditions that allow expression of M. tuberculosis GC.

Editor: R. N. Moore

This article has been cited by other articles:

• Dinadayala, P., Sambou, T., Daffe, M., Lemassu, A. (2008). Comparative structural analyses of the {alpha}-glucan and glycogen from Mycobacterium bovis. Glycobiology 18: 502-508 [Abstract] [Full Text]  
• Wittkowski, M., Mittelstadt, J., Brandau, S., Reiling, N., Lindner, B., Torrelles, J., Brennan, P. J., Holst, O. (2007). Capsular Arabinomannans from Mycobacterium avium with Morphotype-specific Structural Differences but Identical Biological Activity. J. Biol. Chem. 282: 19103-19112 [Abstract] [Full Text]  
• Stokes, R. W., Norris-Jones, R., Brooks, D. E., Beveridge, T. J., Doxsee, D., Thorson, L. M. (2004). The Glycan-Rich Outer Layer of the Cell Wall of Mycobacterium tuberculosis Acts as an Antiphagocytic Capsule Limiting the Association of the Bacterium with Macrophages. Infect. Immun. 72: 5676-5686 [Abstract] [Full Text]  
• Dinadayala, P., Lemassu, A., Granovski, P., Cerantola, S., Winter, N., Daffe, M. (2004). Revisiting the Structure of the Anti-neoplastic Glucans of Mycobacterium bovis Bacille Calmette-Guerin: STRUCTURAL ANALYSIS OF THE EXTRACELLULAR AND BOILING WATER EXTRACT-DERIVED GLUCANS OF THE VACCINE SUBSTRAINS. J. Biol. Chem. 279: 12369-12378 [Abstract] [Full Text]  
• Yagi, T., Mahapatra, S., Mikusova, K., Crick, D. C., Brennan, P. J. (2003). Polymerization of Mycobacterial Arabinogalactan and Ligation to Peptidoglycan. J. Biol. Chem. 278: 26497-26504 [Abstract] [Full Text]