InlB-Dependent Internalization of Listeria Is Mediated by the Met Receptor Tyrosine Kinase
Open accessAbstract
The Listeria monocytogenes surface protein InlB promotes bacterial entry into mammalian cells. Here, we identify a cellular surface receptor required for InlB-mediated entry. Treatment of mammalian cells with InlB protein or infection with L. monocytogenes induces rapid tyrosine phosphorylation of Met, a receptor tyrosine kinase (RTK) for which the only known ligand is Hepatocyte Growth Factor (HGF). Like HGF, InlB binds to the extracellular domain of Met and induces "scattering" of epithelial cells. Experiments with Met-positive and Met-deficient cell lines demonstrate that Met is required for InlB-dependent entry of L. monocytogenes. InlB is a novel Met agonist that induces bacterial entry through exploitation of a host RTK pathway.
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c-Met is known to function as a receptor for L. monocytogenes internalin B (InlB) and mediates endocytosis of this organism.
“c-Met is also known to function as a receptor for L. monocytogenes internalin B (InlB) and mediates the endocytosis of this organism [31].”
From Candida albicans stimulates formation of a multi-receptor complex that mediates epithelial cell invasion during oropharyngeal infection (2023) · cites this paper as [31]
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Bussolino, F., Di Renzo, M. F., Ziche, M., Bocchietto, E., Olivero, M., Naldini, L., Gaudino, G., Tamagnone, L., Coffer, A., & Comoglio, P. M. (1992) · The Journal of cell biology · doi:10.1083/jcb.119.3.629 · Cited by 1,337 · see citing works
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- [1]1. Berger, E.A. ∙ Murphy, P.M. ∙ Farber, J.M. Chemokine receptors as HIV-1 coreceptorsroles in viral entry, tropism, and disease Annu. Rev. Immunol. 1999; 17:657-700 Crossref Scopus (1926) PubMed Google Scholar
- [2]2. Birchmeier, C. ∙ Gherardi, E. Developmental roles of HGF/SF and its receptor, the c-Met tyrosine kinase Trends Cell Biol. 1998; 8:404-410 Full Text Full Text (PDF) Scopus (516) PubMed Google Scholar
- [3]3. Braun, L. ∙ Dramsi, S. ∙ Dehoux, P. ... InlBan invasion protein of Listeria monocytogenes with a novel type of surface association Mol. Microbiol. 1997; 25:285-294 Crossref Scopus (211) PubMed Google Scholar
- [4]4. Braun, L. ∙ Nato, F. ∙ Payrastre, B. ... The 213 amino-acid leucine-rich repeat region of the Listeria monocytogenes InlB protein is sufficient for entry into mammalian cells, stimulation of PI 3-kinase, and membrane ruffling Mol. Microbiol. 1999; 34:10-23 Crossref Scopus (91) PubMed Google Scholar
- [5]5. Braun, L. ∙ Ghebrehiwet, B. ∙ Cossart, P. gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes Embo. J. 2000; 19:1458-1466 Crossref Scopus (261) PubMed Google Scholar
- [7]7. Chirgadze, D.Y. ∙ Hepple, J.P. ∙ Zhou, H. ... Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding Nature Struct. Biol. 1999; 6:72-79 Crossref Scopus (110) PubMed Google Scholar
- [8]8. Cossart, P. ∙ Lecuit, M. Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement - Bacterial factors, cellular ligands and signaling Embo. J. 1998; 17:3797-3806 Crossref Scopus (253) PubMed Google Scholar
- [9]9. Dramsi, S. ∙ Biswas, I. ∙ Maguin, E. ... Entry of L. monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family Mol. Microbiol. 1995; 16:251-261 Crossref Scopus (398) PubMed Google Scholar
- [10]10. Eggleton, P. ∙ Reid, K.B.M. ∙ Tenner, A.J. C1q- how many functions? How many receptors? Trends Cell Biol. 1998; 8:428-431 Full Text Full Text (PDF) Scopus (85) PubMed Google Scholar
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- Authors
- Shen, Y., Naujokas, M., Park, M., & Ireton, K.
- Affiliations
- University of Toronto (CA)
- Royal Victoria Hospital (CA)
- Corresponding author
- Ireton, Keith
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 103
- Issue
- 3
- Pages
- 501-510
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1964562548
- Cited by
- 523
- References
- 1
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 11 · 2023: 25 · 2022: 18 · 2021: 17 · 2020: 18 · 2019: 16 · 2018: 20 · 2017: 18 · 2016: 13 · 2015: 19 · 2014: 30 · 2013: 24 · 2012: 24
- FWCI
- 17.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Listeria monocytogenes in Food Safety
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- Listeria monocytogenes, InlB, MET receptor tyrosine kinase, bacterial internalization, receptor tyrosine kinase signaling, tyrosine phosphorylation, hepatocyte growth factor, host-pathogen interaction, bacterial cell entry
- MeSH terms
- Animals, Bacterial Proteins, Cell Aggregation, Cell Line, Cytoskeletal Proteins, Dose-Response Relationship, Drug, Endocytosis, Epithelial Cells, Humans, Kidney, Kinetics, Ligands, Listeria monocytogenes, Membrane Proteins, Phosphoproteins, Phosphorylation, Precipitin Tests, Protein Binding, Proto-Oncogene Proteins, Signal Transduction, Gene Deletion, Protein Structure, Tertiary, Phosphotyrosine, Proto-Oncogene Proteins c-met, Hepatocytes, Avian Proteins, Ubiquitin-Protein Ligases, Adaptor Proteins, Signal Transducing, Proto-Oncogene Proteins c-cbl
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