scholarly journals Activation of the SspA Serine Protease Zymogen of Staphylococcus aureus Proceeds through Unique Variations of a Trypsinogen-like Mechanism and Is Dependent on Both Autocatalytic and Metalloprotease-specific Processing

2007 ◽  
Vol 282 (47) ◽  
pp. 34129-34138 ◽  
Author(s):  
Nicholas N. Nickerson ◽  
Lata Prasad ◽  
Latha Jacob ◽  
Louis T. Delbaere ◽  
Martin J. McGavin
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease

scholarly journals Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus

Structure ◽  
2018 ◽  
Vol 26 (4) ◽  
pp. 572-579.e4 ◽  
Author(s):  
Natalia Stach ◽  
Magdalena Kalinska ◽  
Michal Zdzalik ◽  
Radoslaw Kitel ◽  
Abdulkarim Karim ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Substrate Specificity ◽  
Serine Protease

scholarly journals Staphylococcus aureus Induces Increased Serine Protease Activity in Keratinocytes

2017 ◽  
Vol 137 (2) ◽  
pp. 377-384 ◽  
Author(s):  
Michael R. Williams ◽  
Teruaki Nakatsuji ◽  
James A. Sanford ◽  
Alison F. Vrbanac ◽  
Richard L. Gallo
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity

scholarly journals Staphylococcal Exfoliative Toxins Cleave α- and β-Melanocyte-Stimulating Hormones

2000 ◽  
Vol 68 (4) ◽  
pp. 2366-2368 ◽  
Author(s):  
James V. Rago ◽  
Gregory M. Vath ◽  
Timothy J. Tripp ◽  
Gregory A. Bohach ◽  
Douglas H. Ohlendorf ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Glutamic Acid ◽  
Crystal Structures ◽  
Serine Protease ◽  
Protease Activity ◽  
Staphylococcal Scalded Skin Syndrome ◽  
Melanocyte Stimulating Hormone ◽  
Causative Agents ◽  
Serine Protease Family ◽  
Stimulating Hormone

ABSTRACT The staphylococcal exfoliative toxins (ETs) A and B (ETA and ETB) are 27-kDa exotoxins produced by certain strains ofStaphylococcus aureus and are the causative agents of staphylococcal scalded-skin syndrome. The crystal structures of the ETs strongly indicate that the proteins are members of the serine protease family of enzymes, although protease activity until now has not yet been conclusively demonstrated. Here, we show that the peptide β-melanocyte-stimulating hormone (β-MSH) is cleaved by ETA and that both ETA and ETB are capable of cleaving α-MSH. Both toxins exhibit cleavage at specific glutamic acid residues in MSH peptides. Moreover, biologically inactive mutants of ETA were incapable of cleaving β-MSH.

scholarly journals Description of Staphylococcus Serine Protease (ssp) Operon in Staphylococcus aureus and Nonpolar Inactivation of sspA-Encoded Serine Protease

2001 ◽  
Vol 69 (1) ◽  
pp. 159-169 ◽  
Author(s):  
Kelly Rice ◽  
Robert Peralta ◽  
Darrin Bast ◽  
Joyce de Azavedo ◽  
Martin J. McGavin
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease ◽  
Cysteine Protease ◽  
Culture Supernatant ◽  
Pleiotropic Effect ◽  
Infection Model ◽  
Gene Encoding ◽  
Growth And Survival ◽  
In Vivo Growth

ABSTRACT Signature tagged mutagenesis has recently revealed that the Ssp serine protease (V8 protease) contributes to in vivo growth and survival of Staphylococcus aureus in different infection models, and our previous work indicated that Ssp could play a role in controlling microbial adhesion. In this study, we describe an operon structure within the ssp locus of S. aureusRN6390. The ssp gene encoding V8 protease is designated assspA, and is followed by sspB, which encodes a 40.6-kDa cysteine protease, and sspC, which encodes a 12.9-kDa protein of unknown function. S. aureus SP6391 is an isogenic derivative of RN6390, in which specific loss of SspA function was achieved through a nonpolar allelic replacement mutation. In addition to losing SspA, the culture supernatant of SP6391 showed a loss of 22- to 23-kDa proteins and the appearance of a 40-kDa protein corresponding to SspB. Although the 40-kDa SspB protein could degrade denatured collagen, our data establish that this is a precursor form which is normally processed by SspA to form a mature cysteine protease. Culture supernatant of SP6391 also showed a new 42-kDa glucosaminidase and enhanced glucosaminidase activity in the 29 to 32 kDa range. Although nonpolar inactivation of sspA exerted a pleiotropic effect, S. aureus SP6391 exhibited enhanced virulence in a tissue abscess infection model relative to RN6390. Therefore, we conclude that SspA is required for maturation of SspB and plays a role in controlling autolytic activity but does not by itself exert a significant contribution to the development of tissue abscess infections.

scholarly journals Staphylococcal serine protease–like proteins are pacemakers of allergic airway reactions to Staphylococcus aureus

2017 ◽  
Vol 139 (2) ◽  
pp. 492-500.e8 ◽  
Author(s):  
Sebastian Stentzel ◽  
Andrea Teufelberger ◽  
Maria Nordengrün ◽  
Julia Kolata ◽  
Frank Schmidt ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease

scholarly journals Decreased Amounts of Cell Wall-Associated Protein A and Fibronectin-Binding Proteins in Staphylococcus aureus sarA Mutants due to Up-Regulation of Extracellular Proteases

2001 ◽  
Vol 69 (8) ◽  
pp. 4742-4748 ◽  
Author(s):  
Anna Karlsson ◽  
Patricia Saravia-Otten ◽  
Karin Tegmark ◽  
Eva Morfeldt ◽  
Staffan Arvidson
Keyword(s):  
Staphylococcus Aureus ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Binding Proteins ◽  
Protein A ◽  
Fold Increase ◽  
Cysteine Proteases ◽  
Extracellular Proteases ◽  
Fibronectin Binding ◽  
Mutant Cells

ABSTRACT Data have been presented indicating that Staphylococcus aureus cell surface protein can be degraded by extracellular proteases produced by the same bacterium. We have found that insarA mutant cells, which produce high amounts of four major extracellular proteases (staphylococcal serine protease [V8 protease] [SspA], cysteine protease [SspB], aureolysin [metalloprotease] [Aur], and staphopain [Scp]), the levels of cell-bound fibronectin-binding proteins (FnBPs) and protein A were very low compared to those of wild-type cells, in spite of unaltered or increased transcription of the corresponding genes. Cultivation ofsarA mutant cells in the presence of the global protease inhibitor α2-macroglobulin resulted in a 16-fold increase in cell-bound FnBPs, indicating that extracellular proteases were responsible for the decreased amounts of FnBPs in sarAmutant cells. The protease inhibitor E64 had no effect on the level of FnBPs, indicating that cysteine proteases were not involved. Inactivation of either ssp or aur in the prototype S. aureus strain 8325-4 resulted in a threefold increase in the amount of cell-bound FnBPs. Inactivation of the same protease genes in a sarA mutant of 8325-4 resulted in a 10- to 20-fold increase in cell-bound protein A. As the serine protease requires aureolysin to be activated, it can thus be concluded that the serine protease is the most important protease in the release of cell-bound FnBPs and protein A.

scholarly journals Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors

2014 ◽  
Vol 111 (36) ◽  
pp. 13187-13192 ◽  
Author(s):  
D. A. C. Stapels ◽  
K. X. Ramyar ◽  
M. Bischoff ◽  
M. von Kockritz-Blickwede ◽  
F. J. Milder ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease ◽  
Protease Inhibitors ◽  
Serine Protease Inhibitors

Virulence gene profiles inStaphylococcus aureusisolated from cows with subclinical mastitis in eastern Poland

2016 ◽  
Vol 83 (2) ◽  
pp. 228-235 ◽  
Author(s):  
Barbara Kot ◽  
Piotr Szweda ◽  
Aneta Frankowska-Maciejewska ◽  
Małgorzata Piechota ◽  
Katarzyna Wolska
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease ◽  
Virulence Genes ◽  
Bovine Mastitis ◽  
Virulence Gene ◽  
Subclinical Mastitis ◽  
Staph Aureus ◽  
Gene Profiles ◽  
Enterotoxin Genes ◽  
Genes Encoding

Staphylococcus aureusis arguably the most important pathogen involved in bovine mastitis. The aim of this study was to determine the virulence gene profiles of 124Staph. aureusisolates from subclinical mastitis in cows in eastern Poland. The presence of 30 virulence genes encoding adhesins, proteases and superantigenic toxins was investigated by PCR. The 17 different combinations of adhesin genes were identified. Occurrence ofeno(91·1%) andfib(82·3%) genes was found to be common. The frequency of other adhesion genesfnbA, fnbB, ebpswere 14·5, 50, 25%, respectively, and forcnaandbbpwere 1·6%. TheetAandetDgenes, encoding exfoliative toxins, were present in genomes of 5·6 and 8·9% isolates, respectively. ThesplAandsspA, encoding serine protease, were detected in above 90% isolates. The most frequent enterotoxin genes weresei(21%),sem(19·4%),sen(19·4%),seg(18·5%) andseo(13·7%). Thetstgene was harboured by 2·4% isolates. The 19 combinations of the superantigenic toxin genes were obtained and found in 35·5% of isolates. Three of them (seg, sei, sem, sen, seo; sec, seg, sei, sem, sen, seoandseg, sei, sem, sen) were the most frequent and found in 16·1% of the isolates. The most common virulotype, present in 17·7% of the isolates, wasfib, eno, fnbB, splA, splE, sspA. The results indicate the variation in the presence of virulence genes inStaph. aureusisolates and considerable diversity of isolates that are able to cause mastitis in cows.

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