Evidence map›Paper›PMID 32951986›Full record

ReviewTrends in microbiology2021

Molecular Evolution of Transition Metal Bioavailability at the Host-Pathogen Interface.

Giuliano T Antelo, Alejandro J Vila, David P Giedroc, Daiana A Capdevila

Open access · greenAbstract readReview
In one paragraph

Review in Trends in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. CorAVeterinary research · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Anti-infective compounds forSustainable microbiology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025
    Article
  13. Compatibility of intracellular binding: Evolutionary design principles for metal sensors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. The Exoproteome and Surfaceome of ToxigenicJournal of proteome research · 2025
    Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Review
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 4 institutions in 2 countries.

Giuliano T AnteloFundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), C1405BWE Ciudad Autónoma de Buenos Aires, Buenos Aires, Argentina.
Alejandro J VilaInstituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR), Ocampo and Esmeralda, S2002LRK Rosario, Argentina; Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, S2002LRK Rosario, Argentina.
David P GiedrocDepartment of Chemistry, Indiana University, Bloomington, IN 47405, USA; Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA. Electronic address: giedroc@indiana.edu.
Daiana A CapdevilaFundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), C1405BWE Ciudad Autónoma de Buenos Aires, Buenos Aires, Argentina. Electronic address: dcapdevila@leloir.org.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARFundación Instituto Leloir · ARIndiana University Bloomington · USInstituto de Biología Molecular y Celular de Rosario · AR

Funding

Transition Metal Homeostasis and Reactive Sulfur Species in Bacterial PathogensR35GM118157 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI DAVID P. GIEDROC · 2016 to 2026
$5.9M
A Mechanism-Based Approach to Metallo-beta-Lactamase InhibitionR01AI100560 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A., SPENCER, JAMES · 2012 to 2022
$4.4M
NIAID NIH HHS R01 AI100560NIGMS NIH HHS R35 GM118157
6 · The paper itself

Abstract

The molecular evolution of the adaptive response at the host-pathogen interface has been frequently referred to as an 'arms race' between the host and bacterial pathogens. The innate immune system employs multiple strategies to starve microbes of metals. Pathogens, in turn, develop successful strategies to maintain access to bioavailable metal ions under conditions of extreme restriction of transition metals, or nutritional immunity. However, the processes by which evolution repurposes or re-engineers host and pathogen proteins to perform or refine new functions have been explored only recently. Here we review the molecular evolution of several human metalloproteins charged with restricting bacterial access to transition metals. These include the transition metal-chelating S100 proteins, natural resistance-associated macrophage protein-1 (NRAMP-1), transferrin, lactoferrin, and heme-binding proteins. We examine their coevolution with bacterial transition metal acquisition systems, involving siderophores and membrane-spanning metal importers, and the biological specificity of allosteric transcriptional regulatory proteins tasked with maintaining bacterial metallostasis. We also discuss the evolution of metallo-β-lactamases; this illustrates how rapid antibiotic-mediated evolution of a zinc metalloenzyme obligatorily occurs in the context of host-imposed nutritional immunity.

Indexed as

Evolution, MolecularBacteriaBacterial ProteinsBiological AvailabilityHost-Pathogen InteractionsHumansMetalsBacterial ProteinsMetalscalprotectinmetalloregulatormetallostasismetallo-β-lactamasesnutritional immunity

Identifiers

PMID32951986
PMCPMC7969482
OpenAlexW3087372680

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.