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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The complexity of the bacterial molecular program required for gaining access to the host intracellular environment is revealed, revealing the role of the internalin family of listerial surface proteins in cellular invasion.
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The ability of this pathogen to multiply in various environments as well as the possibility of its interaction with many kinds of eukaryotic cells is, in fact, made possible by the large number of surface proteins.
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To induce bacterial movement in the cytoplasm, the L. monocytogenes surface protein ActA mimics the activity of the eukaryotic WASP family of proteins to recruit to the bacteria the actin nucleation machinery required for actin polymerization and for the formation of theactin structures that propel the parasite in the cytosol and help it to invade neighbouring cells.
Role of internalin proteins in the pathogenesis of Listeria monocytogenes
TLDR
Mechanisms by which five structurally related proteins of the 'internalin' family of L. monocytogenes interact with distinct host receptors to promote infection of human cells and/or crossing of the intestinal, blood-brain, or placental barriers are discussed.
Classes and functions of Listeria monocytogenes surface proteins.
TLDR
The ability of this pathogen to multiply in various environments as well as the possibility of its interaction with many kinds of eukaryotic cells is, in fact, made possible by the large number of surface proteins.
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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.
E-Cadherin Is the Receptor for Internalin, a Surface Protein Required for Entry of L. monocytogenes into Epithelial Cells
Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells
TLDR
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
TLDR
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.
Interactions of Listeria monocytogenes with mammalian cells during entry and actin‐based movement: bacterial factors, cellular ligands and signaling
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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…
The Sortase SrtA of Listeria monocytogenes Is Involved in Processing of Internalin and in Virulence
TLDR
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.
Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci
ActA from Listeria monocytogenes Can Interact with Up to Four Ena/VASP Homology 1 Domains Simultaneously* 210
TLDR
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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