Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni

Miller, Claire E.; Rock, Jonathan D.; Ridley, Kristian A.; Williams, Peter H.; Ketley, Julian M.

doi:10.1128/jb.01761-07

Cited by 43Salmonella and Campylobacter epidemiologyBacterial Genetics and BiotechnologyIron Metabolism and Disorders

Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni

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Miller, Claire E., Rock, Jonathan D., Ridley, Kristian A., Williams, Peter H., Ketley, Julian M.·2008·Journal of Bacteriology

DOI 10.1128/jb.01761-07PMC PMC2258864

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Abstract

Campylobacter jejuni NCTC 11168 was capable of growth to levels comparable with FeSO4 in defined iron-limited medium (minimal essential medium alpha [MEMalpha]) containing ferrilactoferrin, ferritransferrin, or ferri-ovotransferrin. Iron was internalized in a contact-dependent manner, with 94% of cell-associated radioactivity from either 55Fe-loaded transferrin or lactoferrin associated with the soluble cell fraction. Partitioning the iron source away from bacteria significantly decreased cellular growth. Excess cold transferrin or lactoferrin in cultures containing 55Fe-loaded transferrin or lactoferrin resulted in reduced levels of 55Fe uptake. Growth of C. jejuni in the presence of ferri- and an excess of apoprotein reduced overall levels of growth. Following incubation of cells in the presence of ferrilactoferrin, lactoferrin became associated with the cell surface; binding levels were higher after growth under iron limitation. A strain carrying a mutation in the cj0178 gene from the iron uptake system Cj0173c-Cj0178 demonstrated significantly reduced growth promotion in the presence of ferrilactoferrin in MEMalpha compared to wild type but was not affected in the presence of heme. Moreover, this mutant acquired less 55Fe than wild type when incubated with 55Fe-loaded protein and bound less lactoferrin. Complementation restored the wild-type phenotype when cells were grown with ferrilactoferrin. A mutant in the ABC transporter system permease gene (cj0174c) showed a small but significant growth reduction. The cj0176c-cj0177 intergenic region contains two separate Fur-regulated iron-repressible promoters. This is the first demonstration that C. jejuni is capable of acquiring iron from members of the transferrin protein family, and our data indicate a role for Cj0178 in this process.

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Even without other microbes, C. jejuni can steal iron directly from host lactoferrin and transferrin, a process called iron piracy.
“Even in the absence of other microbes, C. jejuni can steal iron directly from host lactoferrin and transferrin in a process termed iron piracy (Miller et al., 2008).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Miller et al., 2008

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Authors: Miller, C. E., Rock, J. D., Ridley, K. A., Williams, P. H., & Ketley, J. M.
Affiliations: University of Leicester (GB)
Corresponding author: Ketley, Julian M.
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 2008-03-15
Volume: 190
Issue: 6
Pages: 1900-1911
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.01761-07
PMC: PMC2258864
OpenAlex: W2140239247
Cited by: 43
References: 63
Citations by year: 2026: 1 · 2025: 3 · 2024: 2 · 2023: 1 · 2021: 1 · 2020: 4 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 5 · 2014: 3 · 2013: 2 · 2012: 4
FWCI: 5.84
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Leicester Research Archive (University of Leicester) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council (BB/F022328/1)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords: Campylobacter jejuni, lactoferrin, transferrin, iron acquisition, ovotransferrin, iron absorption, ABC transporters, Fur regulation, iron limitation, cell surface binding, heme
MeSH terms: Bacterial Proteins, Cell Division, Conalbumin, Genetic Complementation Test, Humans, Iron, Iron Radioisotopes, Lactoferrin, Mutation, Protein Binding, Transferrin, Gene Expression Regulation, Bacterial, Campylobacter jejuni, Electrophoretic Mobility Shift Assay

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Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni

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