Staphopain A (Staphylococcus aureus): Difference between revisions
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'''Staphopain A''' ({{EC number|3.4.22.48}}, ''ScpA'', ''ScpA<sub>aur</sub>'', ''staphylopain A'', ''staphylococcal cysteine proteinase'') is a secreted [[cysteine protease]] produced by ''[[Staphylococcus aureus]]''. It was first identified in the S. aureus V8 strain as a papain-like cysteine protease. The protease distinguishes itself from the other major proteases of S. aureus in its very broad specificity and its ability to degrade elastin.<ref>{{Cite book|url=http://www.sciencedirect.com/science/article/pii/B978012382219200483X|title=Handbook of Proteolytic Enzymes|last=Kantyka|first=Tomasz|last2=Shaw|first2=Lindsey N.|last3=Potempa|first3=Jan|date=2013-01-01|publisher=Academic Press|isbn=9780123822192|editor-last=Rawlings|editor-first=Neil D.|pages=2150–2157|doi=10.1016/b978-0-12-382219-2.00483-x|editor-last2=Salvesen|editor-first2=Guy}}</ref><ref>{{Cite journal|last=Dubin|first=Grzegorz|date=2002-07-01|title=Extracellular proteases of Staphylococcus spp|url=https://www.ncbi.nlm.nih.gov/pubmed/12437090|journal=Biological Chemistry|volume=383|issue=7-8|pages=1075–1086|doi=10.1515/BC.2002.116|issn=1431-6730|pmid=12437090}}</ref> |
'''Staphopain A''' ({{EC number|3.4.22.48}}, ''ScpA'', ''ScpA<sub>aur</sub>'', ''staphylopain A'', ''staphylococcal cysteine proteinase'') is a secreted [[cysteine protease]] produced by ''[[Staphylococcus aureus]]''. It was first identified in the S. aureus V8 strain as a papain-like cysteine protease. The protease distinguishes itself from the other major proteases of S. aureus in its very broad specificity and its ability to degrade elastin.<ref>{{Cite book|url=http://www.sciencedirect.com/science/article/pii/B978012382219200483X|title=Handbook of Proteolytic Enzymes|last=Kantyka|first=Tomasz|last2=Shaw|first2=Lindsey N.|last3=Potempa|first3=Jan|date=2013-01-01|publisher=Academic Press|isbn=9780123822192|editor-last=Rawlings|editor-first=Neil D.|pages=2150–2157|doi=10.1016/b978-0-12-382219-2.00483-x|editor-last2=Salvesen|editor-first2=Guy}}</ref><ref>{{Cite journal|last=Dubin|first=Grzegorz|date=2002-07-01|title=Extracellular proteases of Staphylococcus spp|url=https://www.ncbi.nlm.nih.gov/pubmed/12437090|journal=Biological Chemistry|volume=383|issue=7-8|pages=1075–1086|doi=10.1515/BC.2002.116|issn=1431-6730|pmid=12437090}}</ref> |
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== Genetics == |
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Staphopain A expressed from the [[gene]] ''scpA'' within the ''scp'' [[operon]]. The operon also contains the gene ''scpB'' for staphostatin A (specific inhibitor of staphopain A), [[Upstream and downstream (DNA)|downstream]] of ''scpA''.<ref>{{Cite journal|last=Filipek|first=Renata|last2=Rzychon|first2=Malgorzata|last3=Oleksy|first3=Aneta|last4=Gruca|first4=Milosz|last5=Dubin|first5=Adam|last6=Potempa|first6=Jan|last7=Bochtler|first7=Matthias|date=2003-10-17|title=The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease|url=https://www.ncbi.nlm.nih.gov/pubmed/12874290|journal=The Journal of Biological Chemistry|volume=278|issue=42|pages=40959–40966|doi=10.1074/jbc.M302926200|issn=0021-9258|pmid=12874290}}</ref><ref name=":0">{{Cite journal|last=Shaw|first=Lindsey|last2=Golonka|first2=Ewa|last3=Potempa|first3=Jan|last4=Foster|first4=Simon J.|date=2004-01-01|title=The role and regulation of the extracellular proteases of Staphylococcus aureus|url=https://www.ncbi.nlm.nih.gov/pubmed/14702415|journal=Microbiology (Reading, England)|volume=150|issue=Pt 1|pages=217–228|doi=10.1099/mic.0.26634-0|issn=1350-0872|pmid=14702415}}</ref> |
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Staphopain A is largely co-expressed with the other three major proteases of ''S. aureus'': [[aureolysin]], [[Glutamyl endopeptidase GluV8|glutamyl endopeptidase]], and staphopain B. The transcription of ''scp'' occurs via a promoter controlled by "[[Housekeeping gene|housekeeping]]" [[sigma factor]] σ<sup>A</sup> and up-regulated by accessory gene regulator ''agr''. It is at also repressed by staphylococcal accessory regulator ''sarA'' and by alternative sigma factor σ<sup>B</sup> (a stress response modulator of [[Gram-positive bacteria]]). ''ssp'' expression is highly expressed in post-exponential growth phase.<ref name=":0" /> A more complex network of modulators and of environmental conditions affecting ''ssp'' expression have been suggested, however. Up-regulation of aureolysin during phagocytosis have also been observed.<ref>{{Cite journal|last=Oscarsson|first=Jan|last2=Tegmark-Wisell|first2=Karin|last3=Arvidson|first3=Staffan|date=2006-10-01|title=Coordinated and differential control of aureolysin (aur) and serine protease (sspA) transcription in Staphylococcus aureus by sarA, rot and agr (RNAIII)|url=https://www.ncbi.nlm.nih.gov/pubmed/16782403|journal=International journal of medical microbiology: IJMM|volume=296|issue=6|pages=365–380|doi=10.1016/j.ijmm.2006.02.019|issn=1438-4221|pmid=16782403}}</ref><ref>{{Cite journal|last=Lindsay|first=J. A.|last2=Foster|first2=S. J.|date=1999-09-01|title=Interactive regulatory pathways control virulence determinant production and stability in response to environmental conditions in Staphylococcus aureus|url=https://www.ncbi.nlm.nih.gov/pubmed/10517329|journal=Molecular & general genetics: MGG|volume=262|issue=2|pages=323–331|issn=0026-8925|pmid=10517329}}</ref> |
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The ''scpA'' gene has a high prevalence in the genome of both [[Commensalism|commensal]]- and [[pathogenic]]-type ''S. aureus'' [[Strains (biology)|strains]].<ref>{{Cite journal|last=Zdzalik|first=Michal|last2=Karim|first2=Abdulkarim Y.|last3=Wolski|first3=Krzysztof|last4=Buda|first4=Pawel|last5=Wojcik|first5=Kinga|last6=Brueggemann|first6=Sarah|last7=Wojciechowski|first7=Piotr|last8=Eick|first8=Sigrun|last9=Calander|first9=Ann-Marie|date=2012-11-01|title=Prevalence of genes encoding extracellular proteases in Staphylococcus aureus - important targets triggering immune response in vivo|url=https://www.ncbi.nlm.nih.gov/pubmed/22762789|journal=FEMS immunology and medical microbiology|volume=66|issue=2|pages=220–229|doi=10.1111/j.1574-695X.2012.01005.x|issn=1574-695X|pmid=22762789}}</ref> |
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{{Cysteine proteases}} |
{{Cysteine proteases}} |
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Revision as of 02:10, 25 March 2017
 | This article needs additional citations for verification. (March 2017) |
| Staphopain A | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.4.22.48 | ||||||||
| CAS no. | 347841-89-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Staphopain A (EC 3.4.22.48, ScpA, ScpAaur, staphylopain A, staphylococcal cysteine proteinase) is a secreted cysteine protease produced by Staphylococcus aureus. It was first identified in the S. aureus V8 strain as a papain-like cysteine protease. The protease distinguishes itself from the other major proteases of S. aureus in its very broad specificity and its ability to degrade elastin.[1][2]
Genetics
Staphopain A expressed from the gene scpA within the scp operon. The operon also contains the gene scpB for staphostatin A (specific inhibitor of staphopain A), downstream of scpA.[3][4]
Staphopain A is largely co-expressed with the other three major proteases of S. aureus: aureolysin, glutamyl endopeptidase, and staphopain B. The transcription of scp occurs via a promoter controlled by "housekeeping" sigma factor σA and up-regulated by accessory gene regulator agr. It is at also repressed by staphylococcal accessory regulator sarA and by alternative sigma factor σB (a stress response modulator of Gram-positive bacteria). ssp expression is highly expressed in post-exponential growth phase.[4] A more complex network of modulators and of environmental conditions affecting ssp expression have been suggested, however. Up-regulation of aureolysin during phagocytosis have also been observed.[5][6]
The scpA gene has a high prevalence in the genome of both commensal- and pathogenic-type S. aureus strains.[7]
- ^ Kantyka, Tomasz; Shaw, Lindsey N.; Potempa, Jan (2013-01-01). Rawlings, Neil D.; Salvesen, Guy (eds.). Handbook of Proteolytic Enzymes. Academic Press. pp. 2150–2157. doi:10.1016/b978-0-12-382219-2.00483-x. ISBN 9780123822192.
- ^ Dubin, Grzegorz (2002-07-01). "Extracellular proteases of Staphylococcus spp". Biological Chemistry. 383 (7–8): 1075–1086. doi:10.1515/BC.2002.116. ISSN 1431-6730. PMID 12437090.
- ^ Filipek, Renata; Rzychon, Malgorzata; Oleksy, Aneta; Gruca, Milosz; Dubin, Adam; Potempa, Jan; Bochtler, Matthias (2003-10-17). "The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease". The Journal of Biological Chemistry. 278 (42): 40959–40966. doi:10.1074/jbc.M302926200. ISSN 0021-9258. PMID 12874290.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b Shaw, Lindsey; Golonka, Ewa; Potempa, Jan; Foster, Simon J. (2004-01-01). "The role and regulation of the extracellular proteases of Staphylococcus aureus". Microbiology (Reading, England). 150 (Pt 1): 217–228. doi:10.1099/mic.0.26634-0. ISSN 1350-0872. PMID 14702415.
- ^ Oscarsson, Jan; Tegmark-Wisell, Karin; Arvidson, Staffan (2006-10-01). "Coordinated and differential control of aureolysin (aur) and serine protease (sspA) transcription in Staphylococcus aureus by sarA, rot and agr (RNAIII)". International journal of medical microbiology: IJMM. 296 (6): 365–380. doi:10.1016/j.ijmm.2006.02.019. ISSN 1438-4221. PMID 16782403.
- ^ Lindsay, J. A.; Foster, S. J. (1999-09-01). "Interactive regulatory pathways control virulence determinant production and stability in response to environmental conditions in Staphylococcus aureus". Molecular & general genetics: MGG. 262 (2): 323–331. ISSN 0026-8925. PMID 10517329.
- ^ Zdzalik, Michal; Karim, Abdulkarim Y.; Wolski, Krzysztof; Buda, Pawel; Wojcik, Kinga; Brueggemann, Sarah; Wojciechowski, Piotr; Eick, Sigrun; Calander, Ann-Marie (2012-11-01). "Prevalence of genes encoding extracellular proteases in Staphylococcus aureus - important targets triggering immune response in vivo". FEMS immunology and medical microbiology. 66 (2): 220–229. doi:10.1111/j.1574-695X.2012.01005.x. ISSN 1574-695X. PMID 22762789.