Cited by 303Listeria monocytogenes in Food SafetyBiochemical and Structural CharacterizationBacterial Genetics and Biotechnology

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Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

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Schubert, Wolf-Dieter, Urbanke, Claus, Ziehm, Thilo, Beier, Viola, Machner, Matthias P., Domann, Eugen, Wehland, Jürgen, Chakraborty, Trinad, Heinz, Dirk W.·2002·Cell

DOI 10.1016/s0092-8674(02)01136-4

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Abstract

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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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.
ORCID: Schubert, Wolf-Dieter
Machner, Matthias P.
Domann, Eugen
Chakraborty, Trinad
Heinz, Dirk W.
Venue: Cell
Publisher: Elsevier BV
Published: 2002-12
Volume: 111
Issue: 6
Pages: 825-836
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(02)01136-4
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3881 d)
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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Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

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