Evidence map›Paper›PMID 26253803›Full record

ArticleJournal of microbiological methods2015

A dual component heme biosensor that integrates heme transport and synthesis in bacteria.

Christopher L Nobles, Justin R Clark, Sabrina I Green, Anthony W Maresso

Abstract read
In one paragraph

Article in Journal of microbiological methods, 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
0.5field-weighted citation impact, top 35% 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.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Porphyrins as Colorimetric and Photometric Biosensors in Modern Bioanalytical Systems.Chembiochem : a European journal of chemical biology · 2020
    Review
  6. Review
  7. Article
  8. Article
  9. 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

4 authors at 1 institution in 1 country.

Christopher L NoblesMolecular Virology and Microbiology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States.
Justin R ClarkMolecular Virology and Microbiology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States.
Sabrina I GreenMolecular Virology and Microbiology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States.
Anthony W MaressoMolecular Virology and Microbiology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States.
Baylor College of Medicine · US

Funding

Novel Platforms for Human Intestinal Enteroids: Matrix, Mechanics, and TopographyU19AI116497 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI GRANDE-ALLEN, KATHRYN JANE · 2015 to 2025
$13.2M
Initiative for Maximizing Student Development (IMSD) ProgramR25GM056929 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI PEREIRA, FRED A · 1998 to 2023
$12.4M
Nutrient Uptake during Anthrax DiseaseR01AI097167 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI MARESSO, ANTHONY W · 2012 to 2022
$3.5M
Branched Chain Amino Acid Metabolism During AnthraxR21AI146481 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI MARESSO, ANTHONY W · 2019 to 2020
$440k
Optical Imaging to Monitor Heme Acquisition during Bacterial InfectionR21AI088329 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI MARESSO, ANTHONY W · 2011 to 2012
$437k
Targeting Heme Transporters for Improved Vaccines against AnthraxR21AI109465 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI MARESSO, ANTHONY W · 2015 to 2016
$435k
Characterization of Heme Acquisition in B. anthracisF32AI069697 · NIAID · UNIVERSITY OF CHICAGO · PI MARESSO, ANTHONY W · 2007 to 2008
$58k
NIAID NIH HHS AI069697NIAID NIH HHS AI116497NIAID NIH HHS F32 AI069697NIAID NIH HHS R01 AI097167NIAID NIH HHS R21 AI088329NIAID NIH HHS R21 AI109465NIAID NIH HHS R21 AI146481NIAID NIH HHS U19 AI116497NIGMS NIH HHS R25 GM056929
6 · The paper itself

Abstract

Bacterial pathogens acquire host iron to power cellular processes and replication. Heme, an iron-containing cofactor bound to hemoglobin, is scavenged by bacterial proteins to attain iron. Methods to measure intracellular heme are laborious, involve complex chemistry, or require radioactivity. Such drawbacks limit the study of the mechanistic steps of heme transport and breakdown. Hypothesizing heme homeostasis could be measured with fluorescent methods, we coupled the conversion of heme to biliverdin IXα (a product of heme catabolism) by heme oxygenase 1 (HO1) with the production of near-infrared light upon binding this verdin by infrared fluorescent protein (IFP1.4). The resultant heme sensor, IFP-HO1, was fluorescent in pathogenic E. coli exposed to heme but not in the absence of the heme transporter ChuA and membrane coupling protein TonB, thereby validating their long-standing proposed role in heme uptake. Fluorescence was abolished in a strain lacking hemE, the central gene in the heme biosynthetic pathway, but stimulated by iron, signifying the sensor reports on intracellular heme production. Finally, an invasive strain of E. coli harboring the sensor was fluorescent during an active infection. This work will allow researchers to expand the molecular toolbox used to study heme and iron acquisition in culture and during infection.

Indexed as

AnimalsBiological TransportBiosensing TechniquesBiosynthetic PathwaysEscherichia coliEscherichia coli InfectionsEscherichia coli ProteinsFluorescenceGene DeletionHemeMice, Inbred C57BLEscherichia coli ProteinsHemeBiosensorEscherichia coli O157:H7HemeIFP1.4IronPathogenesis

Identifiers

PMID26253803
PMCPMC5837058
OpenAlexW1113025070

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.