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

@article{Schubert2002StructureOI,
  title={Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin},
  author={Wolf-Dieter Schubert and Claus Urbanke and T. Ziehm and Viola Beier and Matthias P. Machner and Eugen Domann and J{\"u}rgen Wehland and Trinad Chakraborty and Dirk W. Heinz},
  journal={Cell},
  year={2002},
  volume={111},
  pages={825-836}
}

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References

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Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain.
TLDR
The extended beta-sheet, resulting from the distinctive fusion of the LRR and the Ig-like folds, constitutes an adaptable concave interaction surface, which it is proposed is responsible for the specific recognition of the host cellular binding partners during infection.
Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells
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It is suggested that internalin exposed on the bacterial surface mediates direct contact between the bacterium and the host cell.
Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization
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It is demonstrated for the first time that the internalin protein alone is sufficient to promote internalization into cells expressing its receptor and confers invasiveness to both Enterococcus faecalis and internalin-coated latex beads.
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The picture that emerges is that this bacterium uses general strategies also used by other invasive bacteria but has evolved a panel of specific tools and tricks to exploit mammalian cell functions, which may lead to a better understanding of important questions in cell biology such as ligand receptor signalling and dynamics of actin polymerization in mammalian cells.
A single amino acid in E‐cadherin responsible for host specificity towards the human pathogen Listeria monocytogenes
Human E‐cadherin promotes entry of the bacterial pathogen Listeria monocytogenes into mammalian cells by interacting with internalin (InlA), a bacterial surface protein. Here we show that mouse
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It is demonstrated that srtA of L. monocytogenes acts as a sortase and plays a role in the pathogenicity.
Entry of Listeria monocytogenes into hepatocytes requires expression of InIB, a surface protein of the internalin multigene family
TLDR
Findings indicate that inIB is required for entry of L. monocytogenes into hepatocytes, but not into intestinal epithelial cells; inIB encodes a surface protein; and internalin plays a role for entry into some hepatocyte cell lines.
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A stoichiometric model is formulated to describe how ActA enables Listeria monocytogenes to utilize efficiently resources of the host cell microfilament for its own intracellular motility.
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