Sandbox Reserved 816: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
No edit summary
No edit summary
 
(11 intermediate revisions by 2 users not shown)
Line 7: Line 7:
=='''Introduction'''==
=='''Introduction'''==


'''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene]
'''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
, which is a [http://en.wikipedia.org/wiki/Gram-positive_bacteria  Gram-positive bacterium] human pathogen.  It has 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 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.
'''Internalin K''' is involved in [http://en.wikipedia.org/wiki/Listeria_monocytogenes  Listeria monocytogene] ability to escape from autophagy by recruitment of [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein] to the bacterial surface.




Line 32: Line 30:




'''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.
'''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 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.
'''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]]
[[Image:Internalin.jpg]]
Line 56: Line 54:
<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.  
<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 major vault protein domain.  
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.
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.




<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.


[[Image:Internalin K.jpg]]
[[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.




Line 76: Line 73:
===='''Interaction Internalin K-major vault protein'''====
===='''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 MVP binding. It plays a key role in pathogen intracellular mobility and infection.  
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'''====
===='''Function of internalin K in Listeria monocytogenes'''====
Line 86: Line 83:


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


http://www.rcsb.org/pdb/explore/explore.do?structureId=4L3F
http://www.rcsb.org/pdb/explore/explore.do?structureId=4L3F
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2773623/
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2773623/




<scene name='56/568014/D1/1'>D1</scene>
=='''Protreopedia Page Contributors and Editors'''==
Lecomte Alix
 
Karasiewicz Tania
 
Student 1A ESBS (Promo 2016)
Retrieved from "https://proteopedia.org/Sandbox_Reserved_816"