Evidence map›Paper›PMID 21762531›Full record

ArticleBMC infectious diseases2011

Role of P27 -P55 operon from Mycobacterium tuberculosis in the resistance to toxic compounds.

María V Bianco, Federico C Blanco, Belén Imperiale, Marina A Forrellad, Roxana V Rocha, Laura I Klepp, Angel A Cataldi, Nora Morcillo, Fabiana Bigi

Open access · goldAbstract read
In one paragraph

Article in BMC infectious diseases, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

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  6. Insights onFrontiers in microbiology · 2018
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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

9 authors at 1 institution in 1 country.

María V BiancoInstituto de Biotecnología, CICVyA-INTA, N, Repetto and De los Reseros, Buenos Aires, Argentina.
Federico C Blanco
Belén Imperiale
Marina A Forrellad
Roxana V Rocha
Laura I Klepp
Angel A Cataldi
Nora Morcillo
Fabiana Bigi
National Agricultural Technology Institute · AR

Funding

Deciphering the function of Mce proteins from Mycobacterium tuberculosisR01AI083084 · NIAID · NATIONAL INSTITUTE OF AGRICULTURE TECH · PI BIGI, FABIANA · 2009 to 2012
$348k
NIAID NIH HHS 1R01AI083084-01
6 · The paper itself

Abstract

backgroundThe P27-P55 (lprG-Rv1410c) operon is crucial for the survival of Mycobacterium tuberculosis, the causative agent of human tuberculosis, during infection in mice. P55 encodes an efflux pump that has been shown to provide Mycobacterium smegmatis and Mycobacterium bovis BCG with resistance to several drugs, while P27 encodes a mannosylated glycoprotein previously described as an antigen that modulates the immune response against mycobacteria. The objective of this study was to determine the individual contribution of the proteins encoded in the P27-P55 operon to the resistance to toxic compounds and to the cell wall integrity of M. tuberculosis.

methodIn order to test the susceptibility of a mutant of M. tuberculosis H37Rv in the P27-P55 operon to malachite green, sodium dodecyl sulfate, ethidium bromide, and first-line antituberculosis drugs, this strain together with the wild type strain and a set of complemented strains were cultivated in the presence and in the absence of these drugs. In addition, the malachite green decolorization rate of each strain was obtained from decolorization curves of malachite green in PBS containing bacterial suspensions.

resultsThe mutant strain decolorized malachite green faster than the wild type strain and was hypersensitive to both malachite green and ethidium bromide, and more susceptible to the first-line antituberculosis drugs: isoniazid and ethambutol. The pump inhibitor reserpine reversed M. tuberculosis resistance to ethidium bromide. These results suggest that P27-P55 functions through an efflux-pump like mechanism. In addition, deletion of the P27-P55 operon made M. tuberculosis susceptible to sodium dodecyl sulfate, suggesting that the lack of both proteins causes alterations in the cell wall permeability of the bacterium. Importantly, both P27 and P55 are required to restore the wild type phenotypes in the mutant.

conclusionsThe results clearly indicate that P27 and P55 are functionally connected in processes that involve the preservation of the cell wall and the transport of toxic compounds away from the cells.

Indexed as

OperonAnti-Infective AgentsBacterial ProteinsBlotting, WesternCell MembraneCell SurvivalCell WallDrug Resistance, MicrobialElectrophoresis, Polyacrylamide GelEthambutolEthidiumIsoniazidLipoproteinsMembrane Transport ProteinsMicrobial Sensitivity TestsMutationAnti-Infective AgentsBacterial ProteinsEthambutolEthidiumIsoniazidLipoproteinsmalachite greenMembrane Transport ProteinsP27 protein, MycobacteriumP55 protein, MycobacteriumRosaniline DyesSodium Dodecyl Sulfate

Identifiers

PMID21762531
PMCPMC3146831
OpenAlexW1971687641

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.