Evidence map›Paper›PMID 31534126›Full record

ArticleNature communications2019

Heme and hemoglobin utilization by Mycobacterium tuberculosis.

Avishek Mitra, Ying-Hui Ko, Gino Cingolani, Michael Niederweis

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Rv3839-Rv3840 links the endogenous heme biosynthesis pathway withbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. International journal of nanomedicine · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Heme and immunity: The heme oxygenase dichotomy.Journal of inorganic biochemistry · 2025
    Review
  13. Article
  14. The PE/PPE family proteins ofFrontiers in immunology · 2025
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. AInfection and immunity · 2024
    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 2 institutions in 2 countries.

Avishek MitraDepartment of Microbiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL, 35294, USA.
Ying-Hui KoDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233S. 10th Street, Philadelphia, PA, 19107, USA.
Gino CingolaniDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233S. 10th Street, Philadelphia, PA, 19107, USA. Gino.Cingolani@jefferson.edu.
Michael NiederweisDepartment of Microbiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL, 35294, USA. mnieder@uab.edu.ORCID http://orcid.org/0000-0003-4068-8092
Thomas Jefferson University · USUniversity of Alabama at Birmingham · US

Funding

X-Ray Crystallography and Macromolecular CharacterizationP30CA056036 · NCI · THOMAS JEFFERSON UNIVERSITY · PI DANIEL P SILVER · 1995 to 2026
$94.8M
Heme and hemoglobin utilization by Mycobacterium tuberculosisR01AI137338 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NIEDERWEIS, MICHAEL · 2019 to 2023
$3.3M
A NEW HYBRID DIFFRACTOMETER FOR MACROMOLECULAR CRYSTALLOGRAPHY AND SAXS AT TJUS10OD017987 · OD · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2014 to 2014
$600k
NCI NIH HHS P30 CA056036NIAID NIH HHS R01 AI137338NIH HHS S10 OD017987
6 · The paper itself

Abstract

Iron is essential for growth of Mycobacterium tuberculosis (Mtb), but most iron in the human body is stored in heme within hemoglobin. Here, we demonstrate that the substrate-binding protein DppA of the inner membrane Dpp transporter is required for heme and hemoglobin utilization by Mtb. The 1.27 Å crystal structure of DppA shows a tetrapeptide bound in the protein core and a large solvent-exposed crevice for heme binding. Mutation of arginine 179 in this cleft eliminates heme binding to DppA and prevents heme utilization by Mtb. The outer membrane proteins PPE36 and PPE62 are also required for heme and hemoglobin utilization, indicating that these pathways converge at the cell surface of Mtb. Albumin, the most abundant blood protein, binds heme specifically and bypasses the requirements for PPE36, PPE62 and Dpp. Thus, our study reveals albumin-dependent and -independent heme uptake pathways, highlighting the importance of iron acquisition from heme for Mtb.

Indexed as

AlbuminsAntigens, BacterialBacterial ProteinsCrystallography, X-RayHemeHemoglobinsHumansIronMycobacterium tuberculosisPeriplasmic Binding ProteinsProtein BindingProtein Structure, SecondaryAlbuminsAntigens, BacterialBacterial ProteinsHemeHemoglobinsIronPeriplasmic Binding ProteinsPPE36 protein, Mycobacterium tuberculosisPPE68 protein, Mycobacterium tuberculosis

Identifiers

PMID31534126
PMCPMC6751184
OpenAlexW2973853581

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.