Sandbox Reserved 1091: Difference between revisions

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The ''Aeromonas Sobria Serine Protease'' ASP protein is a '''serine protease''' that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of ''Kex2'' <ref>PMID:2646633</ref> ([[1r64]]), a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.

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 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>

ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunction 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 causes 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''.

== Maturation of ASP==

The precursor of ASP is composed of 624 amino acids. It contains a signal peptide of 24 amino-acids, a catalytic domain, similar to that of subtilisin, and a P domain.

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 a propeptide (such as Kex2) that is involved in the proper folding of the protein.

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

Phrase dans maturation à reformuler … “For maturation of ASP, the first 24 residues of the propeptide are cleaved and although a functional P-domain is reportedly necessary for maturation of the substitution domain in kexins”

Sandbox Reserved 1091: Difference between revisions

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 The ''Aeromonas Sobria Serine Protease'' ASP protein is a '''serine protease''' that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of ''Kex2'' <ref>PMID:2646633</ref> ([[1r64]]), a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.
-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 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>
 ASP is a '''[http://en.m.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunction 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 causes 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''.
+== Maturation of ASP==
+The precursor of ASP is composed of 624 amino acids. It contains a signal peptide of 24 amino-acids, a catalytic domain, similar to that of subtilisin, and a P domain.
 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 a propeptide (such as Kex2) that is involved in the proper folding of the protein.
+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
 Phrase dans maturation à reformuler … “For maturation of ASP, the first 24 residues of the propeptide are cleaved and although a functional P-domain is reportedly necessary for maturation of the substitution domain in kexins”