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== '''Structure of Internalin K''' == | == '''Structure of Internalin K''' == | ||
| - | '''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''. | + | '''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''. |
Revision as of 18:30, 7 January 2014
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Introduction
Internalin K is a protein from Listeria monocytogene , which is a Gram-positive bacterium human pathogen. Its ability to survive in the human intestine and to cross a variety of membranes, including mucosal, intestinal, placental, and blood–brain barriers, allows it to generate illnesses ranging from gastroenteritis in healthy individuals to bacteremia and meningitis in immunocompromised patients, as well as mother-to-child infections. Listeria monocytogene can survive in a variety of cell types and proteins of the internalin family have been shown to play a key role in this survival.
Internalin K is involved in Listeria monocytogene ability to escape from autophagy by recruitment of major vault protein to the bacterial surface.
Structure
Internalin family's generalities
L.monocytogenes uses a lot of virulence factors to initiate infection. Proteins of the internalin's family, virulence factors, plays a key role in the infection's survival in a variety of cell types. They play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. The internalin family uses a binding partner action.
The three-dimensional structure of the internalin family shows that there are modular proteins in order to improve the binding's partner. A common architecture is pointed, the N-terminal domain, also called N-terminal leucine-rich repeats (LRRs). It is composed of 22-residue regions including a β-strand and an helix. The structure is a curved solenoid. LRR is followed by domains in cell signaling and often in bacterial surface attachment. Whereas the C-terminal regions are not similar that contributes the variety of roles. Each internalin plays a specific role in the infection.
Structure of Internalin K
Internalin K is a multi-domain virulence factor. It harbours four domains formed in the shape of "bent arm".
