Evidence map›Paper›PMID 26368558›Full record

ArticlePloS one2015

Mycobacterium tuberculosis Is a Natural Ornithine Aminotransferase (rocD) Mutant and Depends on Rv2323c for Growth on Arginine.

Annegret Hampel, Claudia Huber, Robert Geffers, Marina Spona-Friedl, Wolfgang Eisenreich, Franz-Christoph Bange

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 17 citations in OpenAlex.

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  5. Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Annegret HampelDepartment of Medical Microbiology and Hospital Epidemiology, Medical School Hannover, 30625 Hanover, Germany.
Claudia HuberLehrstuhl für Biochemie, Technische Universität München, Garching, Germany.
Robert GeffersResearch Group Genome Analytics, Helmholtz Center for Infection Research, 38124 Braunschweig, Germany.
Marina Spona-FriedlLehrstuhl für Biochemie, Technische Universität München, Garching, Germany.
Wolfgang EisenreichLehrstuhl für Biochemie, Technische Universität München, Garching, Germany.
Franz-Christoph BangeDepartment of Medical Microbiology and Hospital Epidemiology, Medical School Hannover, 30625 Hanover, Germany.
Technical University of Munich · DEMedizinische Hochschule Hannover · DEHelmholtz Centre for Infection Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis (Mtb) possesses a genetic repertoire for metabolic pathways, which are specific and fit to its intracellular life style. Under in vitro conditions, Mtb is known to use arginine as a nitrogen source, but the metabolic pathways for arginine utilization have not been identified. Here we show that, in the presence of arginine, Mtb upregulates a gene cluster which includes an ornithine aminotransferase (rocD) and Rv2323c, a gene of unknown function. Isotopologue analysis by using 13C- or 15N-arginine revealed that in Mtb arginine is not only used as nitrogen source but also as carbon source for the formation of amino acids, in particular of proline. Surprisingly, rocD, which is widespread in other bacteria and is part of the classical arginase pathway turned out to be naturally deleted in Mtb, but not in non-tuberculous mycobacteria. Mtb lacking Rv2323c showed a growth defect on arginine, did not produce proline from arginine, and incorporated less nitrogen derived from arginine in its core nitrogen metabolism. We conclude that the highly induced pathway for arginine utilization in Mtb differs from that of other bacteria including non-tuberculous mycobacteria, probably reflecting a specific metabolic feature of intracellular Mtb.

Indexed as

MutationArginineBacterial ProteinsMycobacterium tuberculosisOrnithine-Oxo-Acid TransaminaseArginineBacterial ProteinsOrnithine-Oxo-Acid Transaminase

Identifiers

PMID26368558
PMCPMC4569260
OpenAlexW2214205090

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.