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Papain-Like Proteases of Staphylococcus aureus

  • Chapter
Cysteine Proteases of Pathogenic Organisms

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 712))

Abstract

Staphylococcus aureus remains one of the major humanpathogens, causing a number of diverse infections. the growing antibiotic resistance, including vancomycin and methicilin-resistant strains raises the special interest in virulence mechanism of this pathogen. among a number of extracellular virulence factors, S. aureus secretes several proteases of three catalytic classes—metallo, serine and papain-like cysteine proteases. the expression of proteolytic enzymes is strictly controlled by global regulators of virulence factors expression agr and sar and proteases take a role in a phenotype change in postlogarithmic phase of growth. the staphylococcal proteases are secreted as proenzymes and undergo activation in a cascade manner.

Staphopains, two cysteine, papain-like proteases of S. aureus are both ∼20 kDa proteins that have almost identical three-dimensional structures, despite sharing limited primary sequence identity. although staphopain a displays activity similar to cathepsins, recognising hydrophobic residues at P2 position and large charged residues at P1, staphopain B differs significantly, showing significant preference towards β-branched residues at P2 and accepting only small, neutral residues at the P1 position. there is limited data available on the virulence potential of staphopains in in vivo models. However, in vitro experiments have demonstrated a very broad activity of these enzymes, including destruction of connective tissue, disturbance of clotting and kinin systems and direct interaction with host immune cells. Staphopain genes in various staphylococci species are regularly followed by a gene encoding an extremely specific inhibitor of the respective staphopain. This pattern is conserved across species and it is believed that inhibitors (staphostatins) protect the cytoplasm of the cell from premature activation of staphopains during protein folding. Notably, production and activity of staphopains is controlled on each level, from gene expression, through presence of specific inhibitors in cytoplasm, to the cascade-like activation in extracellular environment. Since these systems are highly conserved, this points to the importance of these proteases in the survival and/or pathogenicity of S. aureus.

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Author information

Authors and Affiliations

  1. Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Poland

    Tomasz Kantyka & Jan Potempa

  2. Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA

    Lindsey N. Shaw

  3. Oral Health and Systemic Disease Research Facility, University of Louisville School of Dentistry, Louisville, Kentucky, USA

    Jan Potempa

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  1. Tomasz Kantyka
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  2. Lindsey N. Shaw
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Editors and Affiliations

  1. Infection, Immunity and Innovation (i3) Institute, University of Technology Sydney, Ultimo, Sydney, Australia

    Mark W. Robinson PhD

  2. Institute of Parasitology, McGill University, McDonald Campus, St. Anne de Bellevue, Quebec, Canada

    John P. Dalton PhD

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© 2011 Landes Bioscience and Springer Science+Business Media, LLC

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Kantyka, T., Shaw, L.N., Potempa, J. (2011). Papain-Like Proteases of Staphylococcus aureus . In: Robinson, M.W., Dalton, J.P. (eds) Cysteine Proteases of Pathogenic Organisms. Advances in Experimental Medicine and Biology, vol 712. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8414-2_1

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