This title appears in the Scientific Report :
2007
Please use the identifier:
http://dx.doi.org/10.1074/jbc.M608695200 in citations.
Inactivation of Corynebacterium glutamicum NCgl0452 and the Role of MgtA in the Biosynthesis of a Novel Mannosylated Glycolipid involved in Lipomannan Biosynthesis
Inactivation of Corynebacterium glutamicum NCgl0452 and the Role of MgtA in the Biosynthesis of a Novel Mannosylated Glycolipid involved in Lipomannan Biosynthesis
Mycobacterium tuberculosis PimB has been demonstrated to catalyze the addition of a mannose residue from GDP-mannose to a monoacylated phosphatidyl-myo-inositol mannoside (Ac(1)PIM(1)) to generate Ac(1)PIM(2). Herein, we describe the disruption of its probable orthologue Cg-pimB and the chemical ana...
Saved in:
Personal Name(s): | Tatituri, R. V. V. |
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Illarionov, P. A. / Dover, L. G. / Nigou, J. / Gilleron, M. / Hitchen, P. / Krumbach, K. / Morris, H.R. / Spencer, N. / Dell, A. / Eggeling, L. / Besra, G. S. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | The @journal of biological chemistry, 282 (2007) S. 4561 - 4572 |
Imprint: |
Bethesda, Md.
Soc.
2007
|
Physical Description: |
4561 - 4572 |
DOI: |
10.1074/jbc.M608695200 |
PubMed ID: |
17179146 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Journal of Biological Chemistry
282 |
Subject (ZB): | |
Publikationsportal JuSER |
Mycobacterium tuberculosis PimB has been demonstrated to catalyze the addition of a mannose residue from GDP-mannose to a monoacylated phosphatidyl-myo-inositol mannoside (Ac(1)PIM(1)) to generate Ac(1)PIM(2). Herein, we describe the disruption of its probable orthologue Cg-pimB and the chemical analysis of glycolipids and lipoglycans isolated from wild type Corynebacterium glutamicum and the C. glutamicum::pimB mutant. Following a careful analysis, two related glycolipids, Gl-A and Gl-X, were found in the parent strain, but Gl-X was absent from the mutant. The biosynthesis of Gl-X was restored in the mutant by complementation with either Cg-pimB or Mt-pimB. Subsequent chemical analyses established Gl-X as 1,2-di-O-C(16)/C(18:1)-(alpha-d-mannopyranosyl)-(1-->4)-(alpha-d-glucopyranosyluronic acid)-(1-->3)-glycerol (ManGlcAGroAc(2)) and Gl-A as the precursor, GlcAGroAc(2). In addition, C. glutamicum::pimB was still able to produce Ac(1)PIM(2), suggesting that Cg-PimB catalyzes the synthesis of ManGlcAGroAc(2) from GlcAGroAc(2). Isolation of lipoglycans from C. glutamicum led to the identification of two related lipoglycans. The larger lipoglycan possessed a lipoarabinomannan-like structure, whereas the smaller lipoglycan was similar to lipomannan (LM). The absence of ManGlcA-GroAc(2) in C. glutamicum::pimB led to a severe reduction in LM. These results suggested that ManGlcAGroAc(2) was further extended to an LM-like molecule. Complementation of C. glutamicum::pimB with Cg-pimB and Mt-pimB led to the restoration of LM biosynthesis. As a result, Cg-PimB, which we have assigned as MgtA, is now clearly defined as a GDP-mannose-dependent alpha-mannosyltransferase from our in vitro analyses and is involved in the biosynthesis of ManGlcAGroAc(2). |