Evidence map›Paper›PMID 24530503›Full record

ArticleBiochimica et biophysica acta2014

Antibacterial activity of rifamycins for M. smegmatis with comparison of oxidation and binding to tear lipocalin.

Tamara Staudinger, Bernhard Redl, Ben J Glasgow

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 44% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Interaction of ceramides and tear lipocalin.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Antimycobacterial activity of fruit ofAvicenna journal of phytomedicine
    Article
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

3 authors at 2 institutions in 2 countries.

Tamara StaudingerDepartment of Ophthalmology, Jules Stein Eye Institute, University of California, Los Angeles, 100 Stein Plaza, Rm. B-279, Los Angeles, CA 90095, USA; Department of Pathology and Laboratory Medicine, Jules Stein Eye Institute, University of California, Los Angeles, 100 Stein Plaza, Rm. B-279, Los Angeles, CA 90095, USA; Division of Molecular Biology, Biocenter, Innsbruck Medical University, Innrain 80-82, A-6020 Innsbruck, Austria.
Bernhard RedlDivision of Molecular Biology, Biocenter, Innsbruck Medical University, Innrain 80-82, A-6020 Innsbruck, Austria.
Ben J GlasgowDepartment of Ophthalmology, Jules Stein Eye Institute, University of California, Los Angeles, 100 Stein Plaza, Rm. B-279, Los Angeles, CA 90095, USA; Department of Pathology and Laboratory Medicine, Jules Stein Eye Institute, University of California, Los Angeles, 100 Stein Plaza, Rm. B-279, Los Angeles, CA 90095, USA. Electronic address: bglasgow@mednet.ucla.edu.
Innsbruck Medical University · ATDoheny Eye Institute · US

Funding

Proteins in the Molecular Mechanisms of Tear Film FormationR01EY011224 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GLASGOW, BEN J · 2001 to 2020
$6.8M
PROTEINS IN MOLECULAR MECHANISMS OF TEAR FILM FORMATIONR29EY011224 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GLASGOW, BEN J · 1996 to 2000
$116k
NEI NIH HHS R01 EY011224NEI NIH HHS R29 EY011224
6 · The paper itself

Abstract

A mutant of Mycobacterium smegmatis is a potential class I model substitute for Mycobacterium tuberculosis. Because not all of the rifamycins have been tested in this organism, we determined bactericidal profiles for the 6 major rifamycin derivatives. The profiles closely mirrored those established for M. tuberculosis. Rifalazil was confirmed to be the most potent rifamycin. Because the tuberculous granuloma presents a harshly oxidizing environment we explored the effects of oxidation on rifamycins. Mass spectrometry confirmed that three of the six major rifamycins showed autoxidation in the presence of trace metals. Oxidation could be monitored by distinctive changes including isosbestic points in the ultraviolet-visible spectrum. Oxidation of rifamycins abrogated anti-mycobacterial activity in M. smegmatis. Protection from autoxidation was conferred by binding susceptible rifamycins to tear lipocalin, a promiscuous lipophilic protein. Rifalazil was not susceptible to autoxidation but was insoluble in aqueous solution. Solubility was enhanced when complexed to tear lipocalin and was accompanied by a spectral red shift. The positive solvatochromism was consistent with robust molecular interaction and binding. Other rifamycins also formed a complex with lipocalin, albeit to a lesser extent. Protection from oxidation and enhancement of solubility with protein binding may have implications for delivery of select rifamycin derivatives.

Indexed as

Antitubercular AgentsEscherichia coliHydrophobic and Hydrophilic InteractionsKineticsLipocalinsMicrobial Sensitivity TestsModels, BiologicalMycobacterium smegmatisMycobacterium tuberculosisOxidation-ReductionProtein BindingRecombinant ProteinsRifamycinsSolubilityStructure-Activity RelationshipAntitubercular AgentsKRM 1648LipocalinsRecombinant ProteinsRifamycinsLipocalin-1Mycobacteria smegmatisOxidationRifabutin (PubChem CID: 6323490)RifalazilRifalazil (PubChem CID: 6540558)Rifampin (PubChem CID: 24871024)RifamycinRifamycin S (PubChem CID: 6436726)Rifamycin SV (PubChem CID: 6324616)Rifapentine (PubChem CID: 6323497)Rifaximin (PubChem CID: 6436173)Tear lipocalin

Identifiers

PMID24530503
PMCPMC3992280
OpenAlexW2039207554

What OpenQuestion holds

Textmetadata
LicenceTDM
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.