Sandbox Reserved 1091: Difference between revisions
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The '''peptide bonds''' were shown to be cleaved when two basic residues were in sequence. A Lys residue at positions P1 and P2 relative to the cleavage site is prefered. If an Arg residue is at P4 position the substrate cleavage will be enhanced. <ref>Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,</ref> | The '''peptide bonds''' were shown to be cleaved when two basic residues were in sequence. A Lys residue at positions P1 and P2 relative to the cleavage site is prefered. If an Arg residue is at P4 position the substrate cleavage will be enhanced. <ref>Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,</ref> | ||
Experiments have been done in order to establish the sensitivity of ASP to proteases. In has been found that the ASP protease activity was strongly attenuated by serine protease inhibitors ([http://en.wikipedia.org/wiki/Diisopropyl_fluorophosphate DFP], [http://fr.wikipedia.org/wiki/Fluorure_de_4-(2-aminoéthyl)benzènesulfonyle AEBSF]). Moreover, a soybean [http://en.wikipedia.org/wiki/Trypsin_inhibitor trypsin inhibitor] was shown not to block the proteolytic action of ASP itself but could inhibit the [http://en.m.wikipedia.org/wiki/Vascular_permeability vascular permeability] enhancing activity that follows after injection of ASP into epithelial cells. <ref>Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al. Japan (2002)</ref> | Experiments have been done in order to establish the '''sensitivity of ASP to proteases'''. In has been found that the ASP protease activity was strongly attenuated by serine protease inhibitors ([http://en.wikipedia.org/wiki/Diisopropyl_fluorophosphate DFP], [http://fr.wikipedia.org/wiki/Fluorure_de_4-(2-aminoéthyl)benzènesulfonyle AEBSF]). Moreover, a soybean [http://en.wikipedia.org/wiki/Trypsin_inhibitor trypsin inhibitor] was shown not to block the proteolytic action of ASP itself but could inhibit the [http://en.m.wikipedia.org/wiki/Vascular_permeability vascular permeability] enhancing activity that follows after injection of ASP into epithelial cells. <ref>Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al. Japan (2002)</ref> | ||
The experimental finding suggests that epithelial trypsin-like proteases mediate the reaction causing enhanced vascular permeability. It is likely that ASP stimulates the secretion and maturation of epithelial trypsin proteases, thus enhancing vascular permeability. ASP could stimulate the [http://en.wikipedia.org/wiki/Bradykinin bradykinin]-releasing pathway, thus stimulating mast cells to release histamine and further enhance the vascular permeability. | The experimental finding suggests that epithelial trypsin-like proteases mediate the reaction causing enhanced vascular permeability. It is likely that ASP stimulates the secretion and maturation of epithelial trypsin proteases, thus enhancing vascular permeability. ASP could stimulate the [http://en.wikipedia.org/wiki/Bradykinin bradykinin]-releasing pathway, thus stimulating mast cells to release histamine and further enhance the vascular permeability. | ||
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== Impact on human body == | == Impact on human body == | ||
The predominant infection vector is through exposure to water harbouring ''Aeromonas sobria''. <ref>Joseph, S. W., O. P. Daily, W. S. Hunt, R. J. Seidler, D. A. Allen, and R. R. Colwell. 1979. Aeromonas primary wound '''infection of a diver in polluted waters'''. J. Clin. Microbiol. 10:46-49.</ref> | The '''predominant infection vector''' is through exposure to water harbouring ''Aeromonas sobria''. <ref>Joseph, S. W., O. P. Daily, W. S. Hunt, R. J. Seidler, D. A. Allen, and R. R. Colwell. 1979. Aeromonas primary wound '''infection of a diver in polluted waters'''. J. Clin. Microbiol. 10:46-49.</ref> | ||
The most common form of disease is one where ''A.sobria'' pathogen adheres to the surface of the intestine causing painful diarrhea, also known as [http://en.wikipedia.org/wiki/Gastroenteritis gastroenteritis]. The enterotoxin activity of the [http://en.wikipedia.org/wiki/Hemolysin hemolysin] [http://en.wikipedia.org/wiki/Virulence_factor virulence factors] of ''A.sobria'' contributes to those symptoms. However, the mortality due to intestinal disease type of infection is low compared to the non-intestinal diseases caused by the ''A.sobria'' infection. | The most common form of disease is one where ''A.sobria'' pathogen adheres to the surface of the intestine causing painful diarrhea, also known as [http://en.wikipedia.org/wiki/Gastroenteritis gastroenteritis]. The enterotoxin activity of the [http://en.wikipedia.org/wiki/Hemolysin hemolysin] [http://en.wikipedia.org/wiki/Virulence_factor virulence factors] of ''A.sobria'' contributes to those symptoms. However, the mortality due to intestinal disease type of infection is low compared to the non-intestinal diseases caused by the ''A.sobria'' infection. | ||
Pili facilitate the adherence of ''Aeromonas'' to human buccal cells. <ref>Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,</ref> | Pili facilitate the adherence of ''Aeromonas'' to human buccal cells. <ref>Cleavage specificity of serine protease of Aeromonas sobria, a member of the kexin family of subtilases., H. Kobayashi, Okayama University, Japan,FEMS Microbiology Letters, Volume 256, Issue 1, March 2006, Pages 165–170,</ref> | ||
