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Journal of Bacteriology, November 2005, p. 7283-7291, Vol. 187, No. 21
0021-9193/05/$08.00+0 doi:10.1128/JB.187.21.7283-7291.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Inserm-UMR 570, Unité de Pathogénie des Infections Systémiques, Groupe Avenir, Paris Cedex 15, F-75730, France,1 IPBS-UMR 5089, Toulouse Cedex, F-31062, France2
Received 24 June 2005/ Accepted 28 July 2005
The cell envelope of mycobacteria is a complex structure that plays an important role in the interactions of the cell with its environment and in the protection against the antimicrobial activity of the immune system. Glycopeptidolipids (GPLs) are species- or type species-specific glycolipids that are present at the surface of a number of mycobacteria and that are characterized by a high variability in glycosylation patterns. These GPLs possess various biological activities that depend mostly on the sugars capping the core molecule. In Mycobacterium smegmatis, the GPL core can be substituted by either two or three deoxyhexoses. In this study, we show that Gtf3 is a glycosyltransferase responsible for the synthesis of the triglycosylated GPLs. Biochemical analysis of these molecules, with a combination of mass spectrometry and chemical degradation methods, has shown that they contain three deoxyhexose moieties. The presence of the triglycosylated GPLs is associated with cell surface modifications that lead to a decrease in sliding motility as well as a modification in cellular aggregation and colony appearance on Congo red. Phylogenetic analysis indicated that Gtf3 is a member of a yet-uncharacterized glycosyltransferase family conserved among the mycobacteria.
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