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Protein Expr Purif. 2003 Jan;27(1):75-84.
Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: a model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase.

Kawamura A, Sandy J, Upton A, Noble M, Sim E.

Department of Pharmacology, University of Oxford, Manfield Road, Oxford OX1 3QT, UK.

Arylamine N-acetyltransferase (NAT) acetylates the front-line anti-tuberculosis drug isoniazid (INH) and has been identified in Mycobacterium tuberculosis. A naturally occurring single nucleotide polymorphism (SNP) was recently found in the NAT gene in clinical isolates of M. tuberculosis. The nucleotide change from G-->A (619) produces an amino acid change Gly(207) Arg, which appears to reduce the activity of the NAT from M. tuberculosis (TBNAT). It has not been possible to generate sufficient soluble recombinant TBNAT for 3D structural studies. Therefore, Mycobacterium smegmatis NAT (SMNAT), which has 60% identity to TBNAT and has Gly at 207, was used as a model to investigate the possible structural effects of the G-->A 619 SNP. The mutant form of SMnat (SM207Rnat) was constructed by in vitro site-directed mutagenesis and was heterologously expressed with an N-terminal His tag in Escherichia coli, for comparison with the SMNAT. Both recombinant SMNATs were purified using Ni affinity chromatography and treated with thrombin to cleave the tag. Both proteins were produced with average yields of over 10 mg/L and were active. Substrate specificity and thermal stability of SM207RNAT were assessed and compared with the wild type SMNAT using kinetic assays and circular dichroism spectroscopy. SM207RNAT was crystallised and a data set of 2.00 A resolution was obtained. The SM207RNAT had different substrate specificities to the wild type protein and the 3D structures revealed that the Gly(207) Arg mutation caused slight changes in the orientation of His(203) in SMNAT.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12509987&dopt=Abstract

Biochem Biophys Res Commun. 2003 Feb 7;301(2):558-63.
Conservation and cloning of CYP51: a sterol 14 alpha-demethylase from Mycobacterium smegmatis.

Jackson CJ, Lamb DC, Marczylo TH, Parker JE, Manning NL, Kelly DE, Kelly SL.

Wolfson Laboratory of P450 Biodiversity, Institute of Biological Sciences, University of Wales, Aberystwyth, Wales, SY23 3DA, UK.

The genetic locus encoding cytochrome P450 51 (CYP51; P450(14DM)) in Mycobacterium smegmatis is described here together with confirmation of activity in lanosterol 14 alpha-demethylation. The protein bound azole antifungals with high affinity and the rank order based on affinity matched the ranked order for microbiological sensitivity of the organism, thus supporting a possible role for CYP51 as a target in the antimycobacterial activity of these compounds. Non-saponifiable lipids were extracted from the bacteria grown on minimal medium. Unlike a previous report using growth on complex medium, no cholesterol was detected in two strains of M. smegmatis, but a novel lipid was detected. The genetic locus of CYP51 is discussed in relation to function; it is conserved as part of a putative operon in M. smegmatis, Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium bovis and consists of six open-reading frames including two CYPs and a ferredoxin under a putative Tet-R regulated promoter.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12565899&dopt=Abstract

J Biol Chem. 2003 Mar 7;278(10):8333-9. Epub 2003 Jan 02.
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis.

Cho Y, Sharma V, Sacchettini JC.

Department of Biochemistry and Biophysics, Texas A & M University, College Station 77843-2128, USA.

The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 A resolution and without ligands to 2.7 A resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12511575&dopt=Abstract

Thorax. 1998 Oct;53(10):871-4.
Mycobacterium tuberculosis DNA in tissues affected by sarcoidosis.

Wilsher ML, Menzies RE, Croxson MC.

Department of Respiratory Medicine, Auckland Healthcare Ltd, New Zealand.

BACKGROUND: Although some studies have reported the presence of Mycobacterium tuberculosis (MTb) DNA in tissues affected by sarcoidosis, the data are conflicting. The aim of this study was to collect prospectively tissue from patients with sarcoidosis in whom tuberculosis had been excluded, and to use polymerase chain reaction (PCR) to search for DNA sequences specific for MTb. METHODS: Fresh tissue samples (node or lung biopsy) taken from 23 patients with newly diagnosed sarcoidosis, 10 with other respiratory disease, and four patients with culture positive tuberculosis were analysed using PCR to amplify a 123 bp fragment of IS6110, the insertion element present in MTb, and nested PCR to further amplify an 85 bp sequence within the 123 bp product. DNA was also extracted from formalin fixed tissue from eight additional patients with sarcoidosis. RESULTS: MTb DNA was not detected in any of the tissue samples from patients with sarcoidosis or other respiratory disease but was found in all four patients with tuberculosis. CONCLUSIONS: This study has shown the absence of MTb DNA in lymph node and lung biopsy samples from patients with sarcoidosis. MTb is therefore unlikely to be a factor in the pathogenesis of this disease.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10193375&dopt=Abstract

J Public Health Manag Pract. 1998 May;4(3):1-13.
A model of the cost-effectiveness of directly observed therapy for treatment of tuberculosis.

Palmer CS, Miller B, Halpern MT, Geiter LJ.

MEDTAP International, Bethesda, MD, USA.

A hypothetical cohort of 25,000 TB patients and their contacts were followed for a 10-year period; rates of treatment default, infectiousness following partial treatment, relapse, hospitalization, and development of drug-resistant TB were included. The average cost per case cured was $16,846 with 15% of patients starting DOT, $17,323 with 100% starting DOT, and $20,106 with none starting DOT. The incremental cost per additional case cured was $24,064 when all patients, started treatment on DOT, indicating that outpatient DOT provides a cost-effective method of improving health outcomes for TB patients and their contacts while controlling direct costs.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10186738&dopt=Abstract

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