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Nutritional Immunity: Mechanisms, Host Effectors and Pathogen Bypass Strategies
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Nutritional Immunity: Mechanisms, Host Effectors and Pathogen Bypass Strategies

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Immunology".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 5475

Special Issue Editor

Dr. Laure Yatime

E-Mail Website
Guest Editor
Laboratory of Pathogen-Host Interactions (UMR5235), CNRS / University of Montpellier, Montpellier, France
Interests: protein–protein interactions; X-ray crystallography; structure-based drug design; innate immune system; complement; danger signals; inflammation; RAGE; S100 proteins; immunoglobulin receptors

Special Issue Information

Dear Colleagues,

Nutritional immunity is a defense mechanism by which the host sequesters trace minerals from the extracellular space in order to deprive microbial invaders from essential nutrients and thereby reduce their pathogenecity during infection. This process is orchestrated by a panel of host scavengers that possess high affinity for metal ions, thus being able to efficiently modulate metal concentrations in response to microbial attacks. Many proteic factors are at play to control metal homeostasis in the host, including the well-characterized hepcidin and calprotectin, among others. Unraveling the molecular mechanisms governing metal ion sequestration by these scavengers can provide valuable insights for the design of highly potent antimicrobial agents. On the other hand, pathogens have evolved refined evasion strategies to bypass host immune responses, including the hijacking of these scavengers for efficient ion uptake by ion transporters. This Special Issue on “nutritional immunity” welcomes original research and review articles dealing with these questions, with a strong focus on 1) the host molecular effectors of nutritional immunity; 2) the mechanisms used to efficiently sequester metal ions, including the characterization of the ion binding properties of these scavengers, as well as other mechanisms employed by the host to regulate ion concentrations in response to infections; 3) the evasion strategies elaborated by pathogens and the microbial effectors involved; and 4) drug design strategies that may exploit the action of metal scavengers for antibacterial applications.  

Dr. Laure Yatime
Guest Editor

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Keywords

  • nutritional immunity
  • transition metals
  • metallostasis
  • calprotectin
  • hepcidin
  • metal scavengers
  • metal ion uptake
  • ion transport
  • bacterial evasion mechanisms

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Published Papers (2 papers)

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Research

16 pages, 2955 KiB  
Article
DMT1 Protects Macrophages from Salmonella Infection by Controlling Cellular Iron Turnover and Lipocalin 2 Expression
by Manuel Grander, Alexander Hoffmann, Markus Seifert, Egon Demetz, Philipp Grubwieser, Christa Pfeifhofer-Obermair, David Haschka and Günter Weiss
Int. J. Mol. Sci. 2022, 23(12), 6789; https://doi.org/10.3390/ijms23126789 - 17 Jun 2022
Cited by 16 | Viewed by 2749
Abstract
Macrophages are at the center of innate pathogen control and iron recycling. Divalent metal transporter 1 (DMT1) is essential for the uptake of non-transferrin-bound iron (NTBI) into macrophages and for the transfer of transferrin-bound iron from the endosome to the cytoplasm. As the [...] Read more.
Macrophages are at the center of innate pathogen control and iron recycling. Divalent metal transporter 1 (DMT1) is essential for the uptake of non-transferrin-bound iron (NTBI) into macrophages and for the transfer of transferrin-bound iron from the endosome to the cytoplasm. As the control of cellular iron trafficking is central for the control of infection with siderophilic pathogens such as Salmonella Typhimurium, a Gram-negative bacterium residing within the phagosome of macrophages, we examined the potential role of DMT1 for infection control. Bone marrow derived macrophages lacking DMT1 (DMT1fl/flLysMCre(+)) present with reduced NTBI uptake and reduced levels of the iron storage protein ferritin, the iron exporter ferroportin and, surprisingly, of the iron uptake protein transferrin receptor. Further, DMT1-deficient macrophages have an impaired control of Salmonella Typhimurium infection, paralleled by reduced levels of the peptide lipocalin-2 (LCN2). LCN2 exerts anti-bacterial activity upon binding of microbial siderophores but also facilitates systemic and cellular hypoferremia. Remarkably, nifedipine, a pharmacological DMT1 activator, stimulates LCN2 expression in RAW264.7 macrophages, confirming its DMT1-dependent regulation. In addition, the absence of DMT1 increases the availability of iron for Salmonella upon infection and leads to increased bacterial proliferation and persistence within macrophages. Accordingly, mice harboring a macrophage-selective DMT1 disruption demonstrate reduced survival following Salmonella infection. This study highlights the importance of DMT1 in nutritional immunity and the significance of iron delivery for the control of infection with siderophilic bacteria. Full article
(This article belongs to the Special Issue Nutritional Immunity: Mechanisms, Host Effectors and Pathogen Bypass Strategies)
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15 pages, 2503 KiB  
Article
CtpB Facilitates Mycobacterium tuberculosis Growth in Copper-Limited Niches
by Oliver Shey-Njila, Ahmed F. Hikal, Tuhina Gupta, Kaori Sakamoto, Hind Yahyaoui Azami, Wendy T. Watford, Frederick D. Quinn and Russell K. Karls
Int. J. Mol. Sci. 2022, 23(10), 5713; https://doi.org/10.3390/ijms23105713 - 20 May 2022
Cited by 4 | Viewed by 2266
Abstract
Copper is required for aerobic respiration by Mycobacterium tuberculosis and its human host, but this essential element is toxic in abundance. Copper nutritional immunity refers to host processes that modulate levels of free copper to alternately starve and intoxicate invading microbes. Bacteria engulfed [...] Read more.
Copper is required for aerobic respiration by Mycobacterium tuberculosis and its human host, but this essential element is toxic in abundance. Copper nutritional immunity refers to host processes that modulate levels of free copper to alternately starve and intoxicate invading microbes. Bacteria engulfed by macrophages are initially contained within copper-limited phagosomes, which fuse with ATP7A vesicles that pump in toxic levels of copper. In this report, we examine how CtpB, a P-type ATPase in M. tuberculosis, aids in response to nutritional immunity. In vitro, the induced expression of ctpB in copper-replete medium inhibited mycobacterial growth, while deletion of the gene impaired growth only in copper-starved medium and within copper-limited host cells, suggesting a role for CtpB in copper acquisition or export to the copper-dependent respiration supercomplex. Unexpectedly, the absence of ctpB resulted in hypervirulence in the DBA/2 mouse infection model. As ctpB null strains exhibit diminished growth only in copper-starved conditions, reduced copper transport may have enabled the mutant to acquire a “Goldilocks” amount of the metal during transit through copper-intoxicating environments within this model system. This work reveals CtpB as a component of the M. tuberculosis toolkit to counter host nutritional immunity and underscores the importance of elucidating copper-uptake mechanisms in pathogenic mycobacteria. Full article
(This article belongs to the Special Issue Nutritional Immunity: Mechanisms, Host Effectors and Pathogen Bypass Strategies)
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