Malaria impairs resistance to Salmonella through heme- and heme oxygenase–dependent dysfunctional granulocyte mobilization
Open accessAbstract
In sub-Saharan Africa, invasive nontyphoid Salmonella (NTS) infection is a common and often fatal complication of Plasmodium falciparum infection. Induction of heme oxygenase-1 (HO-1) mediates tolerance to the cytotoxic effects of heme during malarial hemolysis but might impair resistance to NTS by limiting production of bactericidal reactive oxygen species. We show that co-infection of mice with Plasmodium yoelii 17XNL (Py17XNL) and Salmonella enterica serovar Typhimurium 12023 (Salmonella typhimurium) causes acute, fatal bacteremia with high bacterial load, features reproduced by phenylhydrazine-induced hemolysis or hemin administration. S. typhimurium localized predominantly in granulocytes. Py17XNL, phenylhydrazine and hemin caused premature mobilization of granulocytes from bone marrow with a quantitative defect in the oxidative burst. Inhibition of HO by tin protoporphyrin abrogated the impairment of resistance to S. typhimurium by hemolysis. Thus, a mechanism of tolerance to one infection, malaria, impairs resistance to another, NTS. Furthermore, HO inhibitors may be useful adjunctive therapy for NTS infection in the context of hemolysis.
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In experimental malaria, HO-1 induction reduces resistance to NTS by suppressing the granulocyte oxidative burst.
“However, HO-1 induction during experimental malaria impairs resistance to NTS by limiting the oxidative burst of granulocytes. (Cunnington et al., 2012).”
From Iron in infection and immunity (2013) · cites this paper as Cunnington et al., 2012
Heme catabolism and subsequent intracellular iron storage by ferritin confers host protection against the blood stage of Plasmodium infection while increasing susceptibility to intracellular Salmonella.
“For example, heme catabolism by and subsequent intracellular Fe storage by ferritin [54,107] confers host protection against the blood stage of Plasmodium infection while increasing susceptibility to the intracellular bacteria Salmonella [108].”
From The Iron age of host–microbe interactions (2015) · cites this paper as [108]
HO-1 expression is associated with increased susceptibility to Salmonella bacteremia during malaria infection and increased mortality from Salmonella infection in that setting.
“On the other side of the coin, HO-1 expression is associated with increased susceptibility to Salmonella bacteremia during malaria infection, and increased mortality from Salmonella infection in that setting (Cunnington et al., 2012).”
From Heme oxygenase 1 controls early innate immune response of macrophages to<i>Salmonella</i>Typhimurium infection: Heme oxygenase 1 expression affects Salmonella<i>infection</i> (2016) · cites this paper as Cunnington et al., 2012
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- Authors
- Cunnington, A. J., de Souza, J. B., Walther, M., & Riley, E. M.
- Affiliations
- London School of Hygiene & Tropical Medicine (GB)
- National Institutes of Health (US)
- Corresponding author
- Riley, Eleanor M
- Venue
- Nature Medicine
- Published
- 2011-12-18
- Volume
- 18
- Issue
- 1
- Pages
- 120-127
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC3272454
- OpenAlex
- W2092422689
- Cited by
- 231
- References
- 55
- Citations by year
- 2026: 12 · 2025: 10 · 2024: 4 · 2023: 5 · 2022: 9 · 2021: 8 · 2020: 18 · 2019: 11 · 2018: 24 · 2017: 14 · 2016: 19 · 2015: 17 · 2014: 34 · 2013: 27 · 2012: 19
- FWCI
- 25.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- LSHTM Research Online (London School of Hygiene and Tropical Medicine) (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- malaria, Salmonella, non-typhoidal Salmonella, heme oxygenase-1, Plasmodium falciparum, Plasmodium yoelii, Salmonella typhimurium, granulocyte mobilization, respiratory burst, reactive oxygen species, hemolysis, phenylhydrazine, hemin, tin protoporphyrin, co-infection, bacteremia, innate immunity
- MeSH terms
- Animals, Cell Movement, Disease Models, Animal, Granulocytes, Heme, Hemin, Hemolysis, Humans, Malaria, Membrane Proteins, Mice, Inbred C57BL, Phenylhydrazines, Plasmodium yoelii, Salmonella Infections, Salmonella typhimurium, Gene Expression, Bacteremia, Respiratory Burst, Mice, Heme Oxygenase-1, Coinfection, Disease Resistance
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