Journal
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY
Volume 94, Issue 2, Pages 277-287Publisher
SPRINGER
DOI: 10.1007/s10482-008-9243-1
Keywords
Corynebacterium glutamicum; Lipomannan; mannosyltransferase; PimB '
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Funding
- Wellcome Trust [081569/Z/06/Z] Funding Source: Wellcome Trust
- MRC [G9901077] Funding Source: UKRI
- Medical Research Council [G9901077] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
- Medical Research Council [G9901077] Funding Source: Medline
- Wellcome Trust [081569/Z/06/Z] Funding Source: Medline
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The genus Corynebacterium is part of the phylogenetic group nocardioform actinomycetes, which also includes the genus Mycobacterium. Members of this phylogenetic group have a characteristic cell envelope structure, which is dominated by complex lipids and amongst these, lipoglycans are of particular interest. The disruption of NCgl2106 in C. glutamicum resulted in a mutant devoid of monoacylated phosphatidyl-myo-inositol dimannoside (Ac(1)PIM(2)) resulting in the accumulation of Ac(1)PIM(1) and cessation of phosphatidyl-myo-inositol (PI) based lipomannan (Cg-LM, now also termed 'Cg-LM-A') and lipoarabinomannan (Cg-LAM) biosynthesis. Interestingly, SDS-analysis of the lipoglycan fraction from the mutant revealed the synthesis of a single novel lipoglycan, now termed 'Cg-LM-B'. Further chemical analyses established the lipoglycan possessed an alpha-D-glucopyranosyluronic acid-(1 --> 3)-glycerol (GlcAGroAc(2)) based anchor which was then further glycosylated by 8-22 mannose residues, with Man(12-20)GlcAGroAC(2) molecular species being the most abundant, to form a novel lipomannan structure (Cg-LM-B). The deletion of NCgl2106 in C. glutamicum has now provided a useful strain, in addition with a deletion mutant of NCgl0452 in C. glutamicum for the purification of Cg-LM-A and Cg-LM-B. Interestingly, both Cg-LM species induced a similar production of TNF-alpha by a human macrophage cell line suggesting that the phospho-myo-inositol residue of the PI-anchor does not play a key role in lipoglycan pro-inflammatory activity.
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