The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin
Open accessAbstract
Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.
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“Interestingly, this family of proteins includes internalin A of L. monocytogenes, which mediates epithelial cell invasion by binding to E-cadherin [41,44].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [44]
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Bacterial Invasion: The Paradigms of Enteroinvasive Pathogens
Cossart, P., & Sansonetti, P. (2004) · Science · doi:10.1126/science.1090124 · Cited by 1,002
Leucine-rich repeats and pathogen recognition in Toll-like receptors
Bell, J. K., Mullen, G. E. D., Leifer, C. A., Mazzoni, A., Davies, D. R., & Segal, D. M. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00242-4 · Cited by 786
Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria
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Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells
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Listeria monocytogenes: a multifaceted model
Hamon, M. A., Bierne, H., & Cossart, P. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1413 · Cited by 613
Metadata
- Authors
- Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W.
- Affiliations
- Helmholtz Centre for Infection Research (DE)
- Medizinische Hochschule Hannover (DE)
- Justus-Liebig-Universität Gießen (DE)
- Corresponding author
- Heinz, Dirk W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 111
- Issue
- 6
- Pages
- 825-836
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2019496511
- Cited by
- 302
- References
- 55
- Citations by year
- 2026: 14 · 2025: 8 · 2024: 4 · 2023: 11 · 2022: 9 · 2021: 7 · 2020: 7 · 2019: 9 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 15 · 2013: 13 · 2012: 13
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Listeria monocytogenes in Food Safety
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Listeria monocytogenes, internalin A, integrated nested Laplace approximation, E-cadherin, bacterial invasion, host cell receptors, leucine-rich repeat domain, protein-protein interaction, host tropism, host susceptibility to infection, epithelial cell adhesion, crystal structure
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Cloning, Molecular, Cytoplasm, Humans, Intestinal Mucosa, Ions, Leucine, Listeria monocytogenes, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Ultracentrifugation, X-Ray Diffraction, Cadherins, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Crystallography, X-Ray
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