scholarly journals Structure-Function Analysis of Enzymes Involved in the Complex Lipid Cell Wall Synthesis of Mycobacterium Tuberculosis

2008 ◽  
Vol S2 (01) ◽  
pp. 101-102 ◽  
Author(s):  
R. Sankaranarayanan
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Structure Function ◽  
Function Analysis ◽  
Cell Wall Synthesis ◽  
Complex Lipid

scholarly journals Drug Targeting Mycobacterium tuberculosis Cell Wall Synthesis: Development of a Microtiter Plate-Based Screen for UDP-Galactopyranose Mutase and Identification of an Inhibitor from a Uridine-Based Library

2003 ◽  
Vol 47 (1) ◽  
pp. 378-382 ◽  
Author(s):  
Michael S. Scherman ◽  
Katharine A. Winans ◽  
Richard J. Stern ◽  
Victoria Jones ◽  
Carolyn R. Bertozzi ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Drug Targeting ◽  
Enzyme Inhibitor ◽  
Microtiter Plate ◽  
Biosynthetic Enzyme ◽  
Cell Wall Synthesis ◽  
Chemical Library ◽  
Microtiter Plate Assay ◽  
Plate Assay

ABSTRACT A microtiter plate assay for UDP-galactopyranose mutase, an essential cell wall biosynthetic enzyme of Mycobacterium tuberculosis, was developed. The assay is based on the release of tritiated formaldehyde from UDP-galactofuranose but not UDP-galactopyranose by periodate and was used to identify a uridine-based enzyme inhibitor from a chemical library.

Structure–Function Analysis of the Acyl Carrier Protein Synthase (AcpS) from Mycobacterium tuberculosis

2009 ◽  
Vol 393 (4) ◽  
pp. 937-950 ◽  
Author(s):  
Orly Dym ◽  
Shira Albeck ◽  
Yoav Peleg ◽  
Alon Schwarz ◽  
Zippora Shakked ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Structure Function ◽  
Acyl Carrier Protein ◽  
Function Analysis ◽  
Carrier Protein

scholarly journals Mycobacterium tuberculosis Lipomannan Induces Apoptosis and Interleukin-12 Production in Macrophages

2004 ◽  
Vol 72 (4) ◽  
pp. 2067-2074 ◽  
Author(s):  
D. N. Dao ◽  
L. Kremer ◽  
Y. Guérardel ◽  
A. Molano ◽  
W. R. Jacobs ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Function Analysis ◽  
Specific Interaction ◽  
Interleukin 12 ◽  
Mycobacterial Species ◽  
Immunostimulatory Activity ◽  
Mycobacterium Chelonae ◽  
Toll Like Receptor 2 ◽  
Mycobacterial Cell Wall

ABSTRACT The mycobacterial cell wall component lipoarabinomannan (LAM) has been described as a virulence factor of Mycobacterium tuberculosis, and modification of the terminal arabinan residues of this compound with mannose caps (producing mannosyl-capped LAM [ManLAM]) in M. tuberculosis or with phosphoinositol caps (producing phosphoinositol-capped LAM [PILAM]) in Mycobacterium smegmatis has been implicated in various functions associated with these lipoglycans. A structure-function analysis was performed by using LAMs and their biosynthetic precursor lipomannans (LMs) isolated from different mycobacterial species on the basis of their capacity to induce the production of interleukin-12 (IL-12) and/or apoptosis of macrophage cell lines. Independent of the mycobacterial species, ManLAMs did not induce IL-12 gene expression or apoptosis of macrophages, whereas PILAMs induced IL-12 secretion and apoptosis. Interestingly, uncapped LAM purified from Mycobacterium chelonae did not induce IL-12 secretion or apoptosis. Furthermore, LMs, independent of their mycobacterial origins, were potent inducers of IL-12 and apoptosis. The precursor of LM, phosphatidyl-myo-inositol dimannoside, had no activity, suggesting that the mannan core of LM was required for the activity of LM. The specific interaction of LM with Toll-like receptor 2 (TLR-2) but not with TLR-4 suggested that these responses were mediated via the TLR-2 signaling pathway. Our experiments revealed an important immunostimulatory activity of the biosynthetic LAM precursor LM. The ratio of LAM to LM in the cell wall of mycobacteria may be an important determinant of virulence, and enzymes that modify LM could provide targets for development of antituberculosis drugs and for derivation of attenuated strains of M. tuberculosis.

scholarly journals Mycobacterium tuberculosis CwsA Interacts with CrgA and Wag31, and the CrgA-CwsA Complex Is Involved in Peptidoglycan Synthesis and Cell Shape Determination

2012 ◽  
Vol 194 (23) ◽  
pp. 6398-6409 ◽  
Author(s):  
P. Plocinski ◽  
N. Arora ◽  
K. Sarva ◽  
E. Blaszczyk ◽  
H. Qin ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Mutant Strain ◽  
Cell Shape ◽  
Double Mutant ◽  
Bacterial Cell Division ◽  
Cell Wall Synthesis ◽  
Content Type ◽  
Ring Assembly ◽  
Double Mutant Strain

ABSTRACTBacterial cell division and cell wall synthesis are highly coordinated processes involving multiple proteins. Here, we show that Rv0008c, a novel small membrane protein fromMycobacterium tuberculosis, localizes to the poles and on membranes and shows an overall punctate localization throughout the cell. Furthermore, Rv0008c interacts with two proteins, CrgA and Wag31, implicated in peptidoglycan (PG) synthesis in mycobacteria. Deletion of the Rv0008c homolog inM. smegmatis, MSMEG_0023, caused bulged cell poles, formation of rounded cells, and defects in polar localization of Wag31 and cell wall synthesis, with cell wall synthesis measured by the incorporation of the [14C]N-acetylglucosamine cell wall precursor. TheM. smegmatisMSMEG_0023crgAdouble mutant strain showed severe defects in growth, viability, cell wall synthesis, cell shape, and the localization of the FtsZ, FtsI, and Wag31 proteins. The double mutant strain also exhibited increased autolytic activity in the presence of detergents. Because CrgA and Wag31 proteins interact with FtsI individually, we believe that regulated cell wall synthesis and cell shape maintenance require the concerted actions of the CrgA, Rv0008c, FtsI, and Wag31 proteins. We propose that, together, CrgA and Rv0008c, renamed CwsA forcellwall synthesis and cellshape proteinA, play crucial roles in septal and polar PG synthesis and help coordinate these processes with the FtsZ-ring assembly in mycobacteria.

scholarly journals Cell-wall synthesis and ribosome maturation are co-regulated by an RNA switch in Mycobacterium tuberculosis

2018 ◽  
Vol 46 (11) ◽  
pp. 5837-5849 ◽  
Author(s):  
Stefan Schwenk ◽  
Alexandra Moores ◽  
Irene Nobeli ◽  
Timothy D McHugh ◽  
Kristine B Arnvig
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Cell Wall Synthesis ◽  
Rna Switch

ubiA (Rv3806c) encoding DPPR synthase involved in cell wall synthesis is associated with ethambutol resistance in Mycobacterium tuberculosis

Tuberculosis ◽  
2015 ◽  
Vol 95 (2) ◽  
pp. 149-154 ◽  
Author(s):  
Lei He ◽  
Xiaobo Wang ◽  
Peng Cui ◽  
Jialin Jin ◽  
Jiazhen Chen ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Cell Wall Synthesis

scholarly journals Galactosyl Transferases in Mycobacterial Cell Wall Synthesis

2007 ◽  
Vol 190 (3) ◽  
pp. 1141-1145 ◽  
Author(s):  
Martina Beláňová ◽  
Petronela Dianišková ◽  
Patrick J. Brennan ◽  
Gladys C. Completo ◽  
Natisha L. Rose ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Mycobacterium Smegmatis ◽  
Cell Wall Synthesis ◽  
Mycobacterial Cell ◽  
Mycobacterial Cell Wall ◽  
Natural And Synthetic

ABSTRACT Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis, the Mycobacterium tuberculosis Rv3782 ortholog known to be involved in the initial steps of galactan formation, harbors dual β-(1→4) and β-(1→5) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Galf-Galf, serves as a direct substrate for full polymerization catalyzed by another bifunctional Galf transferase, GlfT2, the Rv3808c enzyme.

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