Sandbox Reserved 1091: Difference between revisions

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This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [https://www.msdmanuals.com/ septic shock]. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute ~~multivisceral~~ failure, including the lungs, kidneys and liver, can be observed. <ref>https://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>

This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [https://www.msdmanuals.com/ septic shock]. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>https://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>

ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunctions like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.m.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally, it can cause the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''.

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The '''maturation of ASP''' is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain any propeptide that is involved in the proper folding of the protein. This is a major difference with an other protein, close to ASP : Kex2 ([[1r64]]) <ref>Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)</ref>

The ORF2 protein is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space and more specifically the His595. The P-domain of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 ~~interact~~ with the non mature ASP. In the complex, the active site of ASP is blocked. This ~~protect~~ the protein from degradation by others.

The ORF2 protein is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space and more specifically the His595. The P-domain of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 interacts with the non-mature ASP. In the complex, the active site of ASP is blocked. This protects the protein from degradation by others.

When the complex is formed, it moves to the extracellular space and then it dissociates. The active ASP can dissociate ORF2 and exercise its virulence activity in the cell. <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura T, Murakami Y, Nitta H. Biol. Chem. 398 1055-1068 (2017)</ref>

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The nonintestinal form of the disease reports symptoms such as septicemia, lesions of skin and soft tissues as well as meningitis, often ending fatally.

leading to crucial reduction in tissue perfusion followed by fatal organ disfunction.

leading to a crucial reduction in tissue perfusion followed by fatal organ disfunction.

The ASP induced proteolysis digestion of proteins like kininogen, prothrombin, fibrinogen or prekallikrein at restricted sites generates fragments, expressing their own activity and therefore inducing specific physiological reactions. The kinin system activation for example reduces the blood pressure while the prothrombin system promotes plasma coagulation.

The ASP induced proteolysis digestion of proteins like kininogen, prothrombin, fibrinogen or prekallikrein at restricted sites generates fragments, expressing their own activity and therefore inducing specific physiological reactions. The kinin system activation, for example, reduces the blood pressure while the prothrombin system promotes plasma coagulation.

...

Sandbox Reserved 1091: Difference between revisions

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@@ Line 12: / Line 12: @@
-This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [https://www.msdmanuals.com/ septic shock]. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multivisceral failure, including the lungs, kidneys and liver, can be observed. <ref>https://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>
+This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [https://www.msdmanuals.com/ septic shock]. It is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>https://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>
 ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunctions like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.m.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally, it can cause the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''.
@@ Line 22: / Line 22: @@
 The '''maturation of ASP''' is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain any propeptide that is involved in the proper folding of the protein. This is a major difference with an other protein, close to ASP : Kex2 ([[1r64]]) <ref>Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)</ref>
-The ORF2 protein is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space and more specifically the His595. The P-domain of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 interact with the non mature ASP. In the complex, the active site of ASP is blocked. This protect the protein from degradation by others.
+The ORF2 protein is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space and more specifically the His595. The P-domain of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 interacts with the non-mature ASP. In the complex, the active site of ASP is blocked. This protects the protein from degradation by others.
 When the complex is formed, it moves to the extracellular space and then it dissociates. The active ASP can dissociate ORF2 and exercise its virulence activity in the cell. <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura T, Murakami Y, Nitta H. Biol. Chem. 398 1055-1068 (2017)</ref>
@@ Line 71: / Line 71: @@
 The nonintestinal form of the disease reports symptoms such as septicemia, lesions of skin and soft tissues as well as meningitis, often ending fatally.
-leading to crucial reduction in tissue perfusion followed by fatal organ disfunction.
+leading to a crucial reduction in tissue perfusion followed by fatal organ disfunction.
-The ASP induced proteolysis digestion of proteins like kininogen, prothrombin, fibrinogen or prekallikrein at restricted sites generates fragments, expressing their own activity and therefore inducing specific physiological reactions. The kinin system activation for example reduces the blood pressure while the prothrombin system promotes plasma coagulation.
+The ASP induced proteolysis digestion of proteins like kininogen, prothrombin, fibrinogen or prekallikrein at restricted sites generates fragments, expressing their own activity and therefore inducing specific physiological reactions. The kinin system activation, for example, reduces the blood pressure while the prothrombin system promotes plasma coagulation.
 ...