Molecular Evolution of Transition Metal Bioavailability at the Host-Pathogen Interface.
calprotectin
metallo-β-lactamases
metalloregulator
metallostasis
nutritional immunity
Journal
Trends in microbiology
ISSN: 1878-4380
Titre abrégé: Trends Microbiol
Pays: England
ID NLM: 9310916
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
received:
11
06
2020
revised:
01
08
2020
accepted:
19
08
2020
pubmed:
22
9
2020
medline:
11
11
2021
entrez:
21
9
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32951986
pii: S0966-842X(20)30213-4
doi: 10.1016/j.tim.2020.08.001
pmc: PMC7969482
mid: NIHMS1644697
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Metals
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
441-457Subventions
Organisme : NIAID NIH HHS
ID : R01 AI100560
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM118157
Pays : United States
Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
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