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Relevant bibliographies by topics / M. tuberculosis ArgJ

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Journal articles

Academic literature on the topic 'M. tuberculosis ArgJ'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "M. tuberculosis ArgJ"

1

Pasula, Rajamouli, Paul Wisniowski, and William J. Martin. "Fibronectin Facilitates Mycobacterium tuberculosis Attachment to Murine Alveolar Macrophages." Infection and Immunity 70, no. 3 (2002): 1287–92. http://dx.doi.org/10.1128/iai.70.3.1287-1292.2002.

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ABSTRACT Mycobacterium tuberculosis remains a major cause of pulmonary infection worldwide. Attachment of M. tuberculosis organisms to alveolar macrophages (AMs) represents the earliest phase of primary infection in pulmonary tuberculosis. In this study fibronectin (Fn), an adhesive protein, is shown to bind M. tuberculosis organisms and facilitates attachment of M. tuberculosis to murine AMs. A monoclonal antibody (MAb) specific to the heparin binding domain (HBD) of Fn decreases 125I-Fn binding to M. tuberculosis; whereas MAbs specific to either the cell binding domain (CBD) or the gelatin b

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Qualls, Joseph E., Ashley DeFreitas, Amber M. Smith, Stephanie S. Watowich, and Peter J. Murray. "Direct and indirect type-1 arginase (Arg1) induction following Mycobacterium bovis (BCG) infection (43.1)." Journal of Immunology 182, no. 1_Supplement (2009): 43.1. http://dx.doi.org/10.4049/jimmunol.182.supp.43.1.

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Abstract M. tuberculosis infects lung macrophages (MØs) and evades immune responses by a diverse array of mechanisms. We have recently published that BCG infection triggers a MyD88-dependent Arg1 induction that suppresses NO production from infected MØs. In addition, MØ-specific Arg1 conditional knockout mice were more efficient at clearing M. tuberculosis and BCG. In the present study, we have found that while MyD88 is essential for Arg1 induction following infection, MyD88-/- MØs express robust Arg1 mRNA and protein when stimulated with supernatant from BCG-infected WT MØs. Arg1 induction st

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3

Walter, Nicholas D., Bouke C. de Jong, Benjamin J. Garcia, et al. "Adaptation of Mycobacterium tuberculosis to Impaired Host Immunity in HIV-Infected Patients." Journal of Infectious Diseases 214, no. 8 (2016): 1205–11. http://dx.doi.org/10.1093/infdis/jiw364.

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AbstractBackground. It is unknown whether immunosuppression influences the physiologic state of Mycobacterium tuberculosis in vivo. We evaluated the impact of host immunity by comparing M. tuberculosis and human gene transcription in sputum between human immunodeficiency virus (HIV)–infected and uninfected patients with tuberculosis.Methods. We collected sputum specimens before treatment from Gambians and Ugandans with pulmonary tuberculosis, revealed by positive results of acid-fast bacillus smears. We quantified expression of 2179 M. tuberculosis genes and 234 human immune genes via quantita

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Errey, James C., and John S. Blanchard. "Functional Characterization of a Novel ArgA from Mycobacterium tuberculosis." Journal of Bacteriology 187, no. 9 (2005): 3039–44. http://dx.doi.org/10.1128/jb.187.9.3039-3044.2005.

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ABSTRACT The Mycobacterium tuberculosis gene Rv2747 encodes a novel 19-kDa ArgA that catalyzes the initial step in l-arginine biosynthesis, namely the conversion of l-glutamate to α-N-acetyl-l-glutamate. Initial velocity studies reveal that Rv2747 proceeds through a sequential kinetic mechanism, with Km values of 280 mM for l-glutamine and 150 μM for acetyl-coenzyme A and with a k cat value of 200 min−1. Initial velocity studies with l-glutamate showed that even at concentrations of 600 mM, saturation was not observed. Therefore, only a k cat/Km value of 125 M−1 min−1 can be calculated. Inhibi

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Napolitano, Danielle R., Nira Pollock, Suely S. Kashino, Virmondes Rodrigues, and Antonio Campos-Neto. "Identification of Mycobacterium tuberculosis Ornithine Carboamyltransferase in Urine as a Possible Molecular Marker of Active Pulmonary Tuberculosis." Clinical and Vaccine Immunology 15, no. 4 (2008): 638–43. http://dx.doi.org/10.1128/cvi.00010-08.

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ABSTRACT Although the antigen detection assay has the potential to discriminate active tuberculosis from latent infection, development of such a test for the accurate diagnosis of this serious disease has only recently become a matter of interest. Here we present evidence that a Mycobacterium tuberculosis protein (ornithine carboamyltransferase, coded for by MT_1694; Rv1656 [argF]) is an interesting candidate molecule for this test development. The protein was initially discovered by mass spectroscopy in urine of patients with pulmonary tuberculosis and shown by Western blot analysis to be pre

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Bashiri, Ghader, Laura V. Nigon, Ehab N. M. Jirgis, et al. "Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis." Journal of Biological Chemistry 295, no. 12 (2020): 3759–70. http://dx.doi.org/10.1074/jbc.ra119.012158.

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Menaquinone (vitamin K2) plays a vital role in energy generation and environmental adaptation in many bacteria, including the human pathogen Mycobacterium tuberculosis (Mtb). Although menaquinone levels are known to be tightly linked to the cellular redox/energy status of the cell, the regulatory mechanisms underpinning this phenomenon are unclear. The first committed step in menaquinone biosynthesis is catalyzed by MenD, a thiamine diphosphate–dependent enzyme comprising three domains. Domains I and III form the MenD active site, but no function has yet been ascribed to domain II. Here, we sh

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Nagel, Raimund, Jill Thomas, Faith Adekunle, Francis Mann, and Reuben Peters. "Arginine in the FARM and SARM: A Role in Chain-Length Determination for Arginine in the Aspartate-Rich Motifs of Isoprenyl Diphosphate Synthases from Mycobacterium tuberculosis." Molecules 23, no. 10 (2018): 2546. http://dx.doi.org/10.3390/molecules23102546.

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Isoprenyl chains are found in many important metabolites. These are derived from precursors of the appropriate length produced by isoprenyl diphosphate synthases (IDSs). The human pathogen Mycobacterium tuberculosis makes various isoprenoids/terpenoids, with important roles in their biosynthesis played by two closely related IDSs, encoded by grcC1 (Rv0562) and grcC2 (Rv0989c), with Rv0989c generating the 10-carbon precursor (E)-geranyl diphosphate (GPP), and Rv0562 the 20-carbon precursor (E,E,E)-geranylgeranyl diphosphate (GGPP). Intriguingly, while Rv0562 contains the prototypical trans-IDS

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Billington, O. J., T. D. McHugh, and S. H. Gillespie. "Physiological Cost of Rifampin Resistance Induced In Vitro in Mycobacterium tuberculosis." Antimicrobial Agents and Chemotherapy 43, no. 8 (1999): 1866–69. http://dx.doi.org/10.1128/aac.43.8.1866.

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ABSTRACT Drug-resistant Mycobacterium tuberculosis is a major threat to public health. In clinical practice, a limited number of resistance mutations in a short sequence of the beta subunit of RNA polymerase (encoded by rpoB) have been described. Spontaneous resistance to rifampin was induced in vitro in M. tuberculosis H37Rv (ATCC 9360). Only three resistance patterns could be detected by PCR–single-strand conformation polymorphism analysis. Sequence analysis revealed that Ser531→Leu arose most frequently, followed by His526→Arg and then either His526→Tyr or His526→Asp. The relative Darwinian

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Gao, Lian-Yong, Melissa Pak, Rabab Kish, Kimberly Kajihara, and Eric J. Brown. "A Mycobacterial Operon Essential for Virulence In Vivo and Invasion and Intracellular Persistence in Macrophages." Infection and Immunity 74, no. 3 (2006): 1757–67. http://dx.doi.org/10.1128/iai.74.3.1757-1767.2006.

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ABSTRACT The ability to invade and grow in macrophages is necessary for Mycobacterium tuberculosis to cause disease. We have found a Mycobacterium marinum locus of two genes that is required for both invasion and intracellular survival in macrophages. The genes were designated iipA (mycobacterial invasion and intracellular persistence) and iipB. The iip mutant, which was created by insertion of a kanamycin resistance gene cassette at the 5′ region of iipA, was completely avirulent to zebra fish. Expression of the M. tuberculosis orthologue of iipA, Rv1477, fully complemented the iip mutant for

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Guillemin, Isabelle, Vincent Jarlier, and Emmanuelle Cambau. "Correlation between Quinolone Susceptibility Patterns and Sequences in the A and B Subunits of DNA Gyrase in Mycobacteria." Antimicrobial Agents and Chemotherapy 42, no. 8 (1998): 2084–88. http://dx.doi.org/10.1128/aac.42.8.2084.

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ABSTRACT The in vitro activities of seven quinolones and the sequences of the quinolone resistance-determining regions (QRDR) in the A and B subunits of DNA gyrase were determined for 14 mycobacterial species. On the basis of quinolone activity, quinolones were arranged from that with the greatest to that with the least activity as follows: sparfloxacin, levofloxacin, ciprofloxacin, ofloxacin, pefloxacin, flumequine, and nalidixic acid. Based on MICs, the species could be organized into three groups: resistant (Mycobacterium avium, M. intracellulare, M. marinum,M. chelonae, M. abscessus [oflox

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