This Article 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 Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Behling, C A Articles by Hunter, R L Search for Related Content PubMed PubMed Citation Articles by Behling, C A Articles by Hunter, R L

Development of a trehalose 6,6'-dimycolate model which explains cord formation by Mycobacterium tuberculosis.

Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322.

ABSTRACT

Trehalose 6,6'-dimycolate (TDM) is a glycolipid of mycobacteria that displays an unusual toxicity and has been reported to be a virulence factor for Mycobacterium tuberculosis. Lack of understanding of the toxicity has impeded acceptance of TDM as a virulence factor. We previously reported that the toxicity of TDM depends on its presentation as a surface monolayer consisting of 30% trehalose and 70% exposed mycolic acid moieties. This paper further investigates the structure of the TDM monolayer. It began with the observation that beads coated with TDM, but not with closely related analogs, aggregate to form organized structures resembling the cords of virulent mycobacteria. This implied that the TDM molecules in the monolayer were arranged in an organized structure. This structure was investigated by real-time kinetic microscopy, scanning electron microscopy, and gross observations of the adhesion patterns of TDM-coated beads. In each of these models, the structures induced by TDM differed from those of analogs or other amphiphiles studied. These observations were used to construct a model of the structure of TDM monolayer which envisions linear arrays of TDM molecules arranged in a circumferential pattern on beads with discontinuities only at the two poles.

This article has been cited by other articles:

• Hunter, R. L., Olsen, M., Jagannath, C., Actor, J. K. (2006). Trehalose 6,6'-Dimycolate and Lipid in the Pathogenesis of Caseating Granulomas of Tuberculosis in Mice. Am. J. Pathol. 168: 1249-1261 [Abstract] [Full Text]  
• Hunter, R. L., Olsen, M. R., Jagannath, C., Actor, J. K. (2006). Multiple Roles of Cord Factor in the Pathogenesis of Primary, Secondary, and Cavitary Tuberculosis, Including a Revised Description of the Pathology of Secondary Disease. Annals of Clinical & Laboratory Science 36: 371-386 [Abstract] [Full Text]  
• Park, J. S., Tamayo, M. H., Gonzalez-Juarrero, M., Orme, I. M., Ordway, D. J. (2006). Virulent clinical isolates of Mycobacterium tuberculosis grow rapidly and induce cellular necrosis but minimal apoptosis in murine macrophages. J. Leukoc. Biol. 79: 80-86 [Abstract] [Full Text]  
• Nguyen, L., Chinnapapagari, S., Thompson, C. J. (2005). FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis. J. Bacteriol. 187: 6603-6611 [Abstract] [Full Text]  
• Geisel, R. E., Sakamoto, K., Russell, D. G., Rhoades, E. R. (2005). In Vivo Activity of Released Cell Wall Lipids of Mycobacterium bovis Bacillus Calmette-Guerin Is Due Principally to Trehalose Mycolates. J. Immunol. 174: 5007-5015 [Abstract] [Full Text]  
• Byrd, T. F., Lyons, C. R. (1999). Preliminary Characterization of a Mycobacterium abscessus Mutant in Human and Murine Models of Infection. Infect. Immun. 67: 4700-4707 [Abstract] [Full Text]