The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Helicobacter pylori Perturbs Iron Trafficking in the Epithelium to Grow on the Cell Surface
Open accessAbstract
Helicobacter pylori (Hp) injects the CagA effector protein into host epithelial cells and induces growth factor-like signaling, perturbs cell-cell junctions, and alters host cell polarity. This enables Hp to grow as microcolonies adhered to the host cell surface even in conditions that do not support growth of free-swimming bacteria. We hypothesized that CagA alters host cell physiology to allow Hp to obtain specific nutrients from or across the epithelial barrier. Using a polarized epithelium model system, we find that isogenic ΔcagA mutants are defective in cell surface microcolony formation, but exogenous addition of iron to the apical medium partially rescues this defect, suggesting that one of CagA's effects on host cells is to facilitate iron acquisition from the host. Hp adhered to the apical epithelial surface increase basolateral uptake of transferrin and induce its transcytosis in a CagA-dependent manner. Both CagA and VacA contribute to the perturbation of transferrin recycling, since VacA is involved in apical mislocalization of the transferrin receptor to sites of bacterial attachment. To determine if the transferrin recycling pathway is involved in Hp colonization of the cell surface, we silenced transferrin receptor expression during infection. This resulted in a reduced ability of Hp to colonize the polarized epithelium. To test whether CagA is important in promoting iron acquisition in vivo, we compared colonization of Hp in iron-replete vs. iron-deficient Mongolian gerbils. While wild type Hp and ΔcagA mutants colonized iron-replete gerbils at similar levels, ΔcagA mutants are markedly impaired in colonizing iron-deficient gerbils. Our study indicates that CagA and VacA act in concert to usurp the polarized process of host cell iron uptake, allowing Hp to use the cell surface as a replicative niche.
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“H. pylori subsequently acquires iron from transferrin and reveals how H. pylori manipulates host iron metabolism under iron-deplete conditions to promote survival in the stomach.”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Tan et al., 2011
In the citing paper
“CagA causes the mislocalization of transferrin receptors from the basolateral membrane to the apical surface where the pathogen is located (Tan et al., 2011).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Tan et al., 2011
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“H. pylori subsequently acquires iron from transferrin”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Tan et al., 2011
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Metadata
- Authors
- Tan, S., Noto, J. M., Romero-Gallo, J., Peek, R. M., & Amieva, M. R.
- Affiliations
- Stanford University (US)
- Vanderbilt University (US)
- Corresponding author
- Amieva, Manuel R.
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2011-05-12
- Volume
- 7
- Issue
- 5
- Pages
- e1002050
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC3093365
- OpenAlex
- W2079054594
- Cited by
- 175
- References
- 95
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 4 · 2023: 6 · 2022: 9 · 2021: 14 · 2020: 15 · 2019: 8 · 2018: 8 · 2017: 15 · 2016: 17 · 2015: 17 · 2014: 12 · 2013: 18 · 2012: 13
- FWCI
- 15.07
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institutes of Health (CA-77955)
- National Cancer Institute (R29CA077955, CA 92229, CA-77955, CA116837, R01CA092229, R01CA077955)
- National Institute of Allergy and Infectious Diseases (R01AI038459, AI038459)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK058587, DK-58587)
- Topics
- Health Sciences › Medicine › Gastroenterology › Helicobacter pylori-related gastroenterology studies
- Health Sciences › Medicine › Gastroenterology › Gastrointestinal motility and disorders
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- Helicobacter pylori, CagA, VacA, iron acquisition, transferrin, transferrin receptor, transcytosis, iron trafficking, host-pathogen interaction, iron deficiency, Mongolian gerbil, bacterial effector proteins
- MeSH terms
- Adaptation, Physiological, Animals, Antigens, Bacterial, Bacterial Adhesion, Bacterial Proteins, Cell Line, Cell Membrane, Dogs, Epithelium, Gastric Mucosa, Gerbillinae, Humans, Intercellular Junctions, Iron, Receptors, Transferrin, Transferrin, Signal Transduction, Down-Regulation, Helicobacter pylori, Helicobacter Infections, Cell Polarity, Sequence Deletion, Caco-2 Cells, Transcytosis
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