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'''

== ~~Introduction~~ ==

'''

'''~~Internalin K~~''' ~~is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene]~~

=='''Introduction'''==

, 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. [http://en.wikipedia.org/wiki/Listeria_monocytogenes 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.

'''The three-dimensional strsuctures of internalin protein''' have revealed a common N-terminal with leucine-rich repeats (LRRs). Their C-terminal is distinct and implies the specific role of the internalin. Among those proteins, '''Internalin K'''~~, outcome of gene lmo1290 in~~ [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene], is a ~~surface~~-~~associated molecule that can interact with~~ [http://en.wikipedia.org/wiki/~~Major_vault_protein major vault protein~~], a ~~cytoplasmic rubonucleoprotein particle.~~

'''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] which is a [http://en.wikipedia.org/wiki/Gram-positive_bacteria Gram-positive bacterium] human pathogen. Its the 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.These pathologies are caused by the unusual capacity of the bacterium to cross three host barriers during infection and to invade nonphagocytic cells. [http://en.wikipedia.org/wiki/Listeria_monocytogenes 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 a four-domain protein with a “bent arm” morphology. The recognition of [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein] domain is locatized at the “elbow” region.

'''Internalin K''' is involved in [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] ability to escape from autophagy by recruitment of <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> to the bacterial surface.

~~<Structure load='4l3a' size='500' frame='true' align='right' caption='Internalin K dimer' scene='Insert optional scene name here' />~~

~~[http://en.wikipedia.org/wiki/Major_vault_protein major vault protein]~~

~~[http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene]~~

=='''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 there are 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 link with the 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.

[[Image:Internalin.jpg]]

Internalin family

----

Structural comparison of the regions that follow the LRR domains in Internalin K (yellow) shows that Internalin K has a more complex fold.

==== '''Structure of Internalin K''' ====

[[Image:Chain2.png | right]]

'''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''.

Domains <scene name='56/568014/D1/1'>D1</scene> and <scene name='56/568014/D2/1'>D2</scene> are related to domains <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene> by an 90° angle.

The <scene name='56/568014/D1/1'>D1</scene> domain composed of a two-helical cap region and also by the leucine-rich repeats (LRRs). It is stably associated to <scene name='56/568014/D2/1'>D2</scene>.

<scene name='56/568014/D2/1'>D2</scene> has few contacts with <scene name='56/568014/D3/1'>D3</scene> which improves the flexibility required by '''Internalin K''' to bind to its partner while remaining associated to the surface of the bacterium.

The association of <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D2/1'>D2</scene> domains represent the "elbow" region. It means the recognition of <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> domain.

Domains <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene>, located in tandem and related to each other by an approximate 2-fold axis, both fold into compact structures composed of three antiparallel strands packed against two small helices. There are [http://en.wikipedia.org/wiki/Immunoglobulin_superfamily immunoglobulin]-like domain.

[[Image:Internalin K.jpg]]

<scene name='56/568014/D1/1'>D1</scene> and <scene name='56/568014/D2/1'>D2</scene> are involved in binding to protein partners while <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene> most probably serve as pedestals. The flexibility between domains of its elongated structure may play a key role in this complex function.

=='''Function of internalin K'''==

===='''Interaction Internalin K-major vault protein'''====

The surface-associated '''Internalin K''' with Major Vault Protein escapes to ubiquitination and autophagic recognition processes. It means that the recruitment of major vault protein avoids autophagy. MVP is the largest cytoplasmic ribonucleoprotein particle known and is higly abundant in the cytoplasm of eukaryotic cell. The interaction between '''Internalin K''' and MVP could be facilitated by''' internalin K's''' notable structural flexibility. This flexibility is essential for <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> binding. It plays a key role in pathogen intracellular mobility and infection.

===='''Function of internalin K in Listeria monocytogenes'''====

'''Internalin K''' is the first internalin identified as being important for concealment of the pathogen from the eukaryotic defense system rather than cellular entry. The flexible structure permits concealment from recognition by molecules involved in the autophagy process. '''Internalin K''' has a key role in Listeria monocytogenes infection, it is involved in the survival of the [http://en.wikipedia.org/wiki/Gram-positive_bacteria Gram-positive bacterium] by avoided its destruction.

=='''References'''==

1. David Neves1,Viviana Job,Laurent Dortet,Pascale Cossart,Andréa Dessen,Structure of Internalin InlK from the Human Pathogen Listeria monocytogenes, J Mol Biol (2013). http://dx.doi.org/10.1016/j.jmb.2013.08.010

2. Matteo Bonazzi,Marc Lecuit,Pascale Cossart,Listeria monocytogenes Internalin and E-cadherin: From Bench to Bedside. Cold Spring Harb Perspect Biol. 2009 October.PMCID: PMC2773623 doi: 10.1101/cshperspect.a003087

=='''External Ressources'''==

http://www.rcsb.org/pdb/explore/explore.do?structureId=4L3F

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2773623/

=='''Protreopedia Page Contributors and Editors'''==

Lecomte Alix

Karasiewicz Tania

Student 1A ESBS (Promo 2016)

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 <!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-'''
+<Structure load='4l3a' size='500' frame='true' align='right' caption='Internalin K bound to MVP' scene='Insert optional scene name here' />
-== Introduction ==
-'''
-'''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene]
+=='''Introduction'''==
-, 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. [http://en.wikipedia.org/wiki/Listeria_monocytogenes  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.
-'''The three-dimensional strsuctures of internalin protein''' have revealed a common N-terminal with leucine-rich repeats (LRRs). Their C-terminal is distinct and implies the specific role of the internalin. Among those proteins, '''Internalin K''', outcome of gene lmo1290 in [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene], is a surface-associated molecule that can interact with [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein], a cytoplasmic rubonucleoprotein particle.
+'''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene] which is a [http://en.wikipedia.org/wiki/Gram-positive_bacteria  Gram-positive bacterium] human pathogen.  Its the 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.These pathologies are caused by the unusual capacity of the bacterium to cross three host barriers during infection and to invade nonphagocytic cells. [http://en.wikipedia.org/wiki/Listeria_monocytogenes  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 a four-domain protein with a “bent arm” morphology. The recognition of [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein] domain is locatized at the “elbow” region.
+'''Internalin K''' is involved in [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene] ability to escape from autophagy by recruitment of <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> to the bacterial surface.
-<Structure load='4l3a' size='500' frame='true' align='right' caption='Internalin K dimer' scene='Insert optional scene name here' />
-[http://en.wikipedia.org/wiki/Major_vault_protein major vault protein]
-[http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene]
-<scene name='56/568014/Major_vault_protein/1'>MVP</scene>
+=='''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 there are 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 link with the 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.
+[[Image:Internalin.jpg]]
+Internalin family
+----
+Structural comparison of the regions that follow the LRR domains in Internalin K (yellow) shows that Internalin K has a more complex fold.
+==== '''Structure of Internalin K''' ====
+[[Image:Chain2.png | right]]
+'''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''.
+Domains <scene name='56/568014/D1/1'>D1</scene> and <scene name='56/568014/D2/1'>D2</scene> are related to domains <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene> by an 90° angle.
+The <scene name='56/568014/D1/1'>D1</scene> domain composed of a two-helical cap region and also by the leucine-rich repeats (LRRs). It is stably associated to <scene name='56/568014/D2/1'>D2</scene>.
+<scene name='56/568014/D2/1'>D2</scene> has few contacts with <scene name='56/568014/D3/1'>D3</scene> which improves the flexibility required by '''Internalin K''' to bind to its partner while remaining associated to the surface of the bacterium.
+The association of <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D2/1'>D2</scene> domains represent the "elbow" region. It means the recognition of <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> domain.
+Domains <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene>, located in tandem and related to each other by an approximate 2-fold axis, both fold into compact structures composed of three antiparallel strands packed against two small helices. There are [http://en.wikipedia.org/wiki/Immunoglobulin_superfamily immunoglobulin]-like domain.
+[[Image:Internalin K.jpg]]
+<scene name='56/568014/D1/1'>D1</scene> and <scene name='56/568014/D2/1'>D2</scene> are involved in binding to protein partners while <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene> most probably serve as pedestals. The flexibility between domains of its elongated structure may play a key role in this complex function.
+=='''Function of internalin K'''==
+===='''Interaction Internalin K-major vault protein'''====
+The surface-associated '''Internalin K''' with Major Vault Protein escapes to ubiquitination and autophagic recognition processes. It means that the recruitment of major vault protein avoids autophagy. MVP is the largest cytoplasmic ribonucleoprotein particle known and is higly abundant in the cytoplasm of eukaryotic cell. The interaction between '''Internalin K''' and MVP could be facilitated by''' internalin K's'''  notable structural flexibility. This flexibility is essential for <scene name='56/568014/Major_vault_protein/2'>major vault protein</scene> binding. It plays a key role in pathogen intracellular mobility and infection.
+===='''Function of internalin K in Listeria monocytogenes'''====
+'''Internalin K''' is the first internalin identified as being important for concealment of the pathogen from the eukaryotic defense system rather than cellular entry. The flexible structure permits concealment from recognition by molecules involved in the autophagy process. '''Internalin K''' has a key role in Listeria monocytogenes infection, it is involved in the survival of the [http://en.wikipedia.org/wiki/Gram-positive_bacteria  Gram-positive bacterium] by avoided its destruction.
+=='''References'''==
+. David Neves1,Viviana Job,Laurent Dortet,Pascale Cossart,Andréa Dessen,Structure of Internalin InlK from the Human Pathogen Listeria                  monocytogenes, J Mol Biol (2013). http://dx.doi.org/10.1016/j.jmb.2013.08.010
+. Matteo Bonazzi,Marc Lecuit,Pascale Cossart,Listeria monocytogenes Internalin and E-cadherin: From Bench to Bedside. Cold Spring Harb Perspect Biol. 2009 October.PMCID: PMC2773623 doi: 10.1101/cshperspect.a003087
+=='''External Ressources'''==
+http://www.rcsb.org/pdb/explore/explore.do?structureId=4L3F
+http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2773623/
+=='''Protreopedia Page Contributors and Editors'''==
+Lecomte Alix
+Karasiewicz Tania
+Student 1A ESBS (Promo 2016)