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2014 | 61 | 1 | 149-152
Article title

Evaluation of P1' substrate specificity of staphylococcal SplB protease

Content
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EN
Abstracts
EN
Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role. Amid staphylococcal extracellular proteases, those encoded by the spl operon remain poorly characterized, both in terms of enzymology and their physiological role. Initial data demonstrated that Spl proteases exhibit restricted substrate specificity. This study describes development of convenient protein FRET substrates for SplB protease and characterization of the substrate preference of the protease at the P1' position. Kinetic data on hydrolysis of a panel of substrates substituted at the said position is provided.
Publisher

Year
Volume
61
Issue
1
Pages
149-152
Physical description
Dates
published
2014
received
2013-10-30
revised
2014-02-19
accepted
2014-02-20
(unknown)
2014-03-20
Contributors
  • Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
author
  • Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
author
  • Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
  • Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
References
  • Archer GL (1998) Staphylococcus aureus: a well-armed pathogen. Clin Infect Dis 26: 1179-1181.
  • Dubin G (2002) Extracellular proteases of Staphylococcus spp. Biol Chem 383: 1075-1086.
  • Dubin G, Stec-Niemczyk J, Kisielewska M, Pustelny K, Popowicz GM, Bista M, Kantyka T, Boulware KT, Stennicke HR, Czarna A, Phopaisarn M, Daugherty PS, Thogersen IB, Enghild JJ, Thornberry N, Dubin A, Potempa J (2008) Enzymatic activity of the Staphylococcus aureus SpIB serine protease is induced by substrates containing the sequence Trp-Glu-Leu-Gln. J Mol Biol 379: 343-356.
  • Felber LM, Cloutier SM, Kundig C, Kishi T, Brossard V, Jichlinski P, Leisinger HJ, Deperthes D (2004) Evaluation of the CFP-substrate-YFP system for protease studies: advantages and limitations. Biotechniques 36: 878-885.
  • Kolar SL, Ibarra JA, Rivera FE, Mootz JM, Davenport JE, Stevens SM, Horswill AR, Shaw LN (2013) Extracellular proteases are key mediators of Staphylococcus aureus virulence via the global modulation of virulence-determinant stability. Microbiologyopen 2: 18-34.
  • Laskar A, Rodger EJ, Chatterjee A, Mandal C (2012) Modeling and structural analysis of PA clan serine proteases. BMC Res Notes 5: 256.
  • Noble WC (1998) Skin bacteriology and the role of Staphylococcus aureus in infection. Br J Dermatol 139 (Suppl 53): 9-12.
  • Rawlings ND, Barrett AJ, Bateman A (2010) MEROPS: the peptidase database. Nucleic Acids Res 38 (Database issue): D227-D233.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv61p149kz
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