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

• Published in: Cell Vol. 111; no. 6; pp. 825 - 836
• Main Authors: Schubert, Wolf-Dieter, Urbanke, Claus, Ziehm, Thilo, Beier, Viola, Machner, Matthias P., Domann, Eugen, Wehland, Jürgen, Chakraborty, Trinad, Heinz, Dirk W.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 13.12.2002
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Cadherins - chemistry; Cloning, Molecular; Crystallography, X-Ray; Cytoplasm - metabolism; Humans; Intestinal Mucosa - metabolism; Ions; Leucine - chemistry; Listeria monocytogenes - chemistry; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Ultracentrifugation; X-Ray Diffraction

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-cad...