Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus

Björklind, Anders; Jörnvall, Hans

doi:10.1016/0005-2744(74)90113-2

Cited by 41 publications

(24 citation statements)

References 20 publications

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“…In the absence of any other specific candidates it is possible that ScpA achieves activation in an auto-catalytic manner. ScpA has a very broad substrate range with no preference in cleavage recognition site (Bjoorklind & Jornvall, 1974). Furthermore, it is relatively common for papain-like proteases to undergo auto-catalytic maturation , as is the case with the cysteine protease streptopain from Streptococcus pyogenes (Elliott, 1945;Liu & Elliott, 1965;Rasmussen & Bjorck, 2002).…”

Section: Discussionmentioning

confidence: 99%

The role and regulation of the extracellular proteases of Staphylococcus aureus

et al. 2004

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Staphylococcus aureus has several extracellular proteases with proposed roles in virulence. SspA (serine protease), SspB (cysteine protease) and Aur (metalloprotease) have been characterized previously and SspA and SspB were found to be cotranscribed. The coding region for the cysteine protease ScpA has been identified and characterized. It is in a probable bi-cistronic operon with scpA located immediately upstream of a coding region for a 108 aa protein that is a specific inhibitor of ScpA. Using primer extension analysis promoters have been mapped and it was found that s A is the only sigma factor involved in the transcription of scpA, sspABC and aur. The transcription of all the genes occurs maximally at post-exponential phase, being positively regulated by agr (accessory gene regulator) and negatively regulated by sarA (staphylococcal accessory regulator). Although the metalloprotease, Aur, does catalyse activation of the SspA zymogen, it is not the sole agent capable of conducting this process. Site-directed mutagenesis revealed that Aur is not capable of undergoing auto-proteolysis to achieve activation. The cysteine protease, ScpA, appears to reside outside this cascade of activation, as mature ScpA was observed in the aur, sspA and sspB mutant strains. Using a mouse abscess model, it has been shown that insertional inactivation of sspA or sspB results in significant attenuation of virulence, whilst mutations in aur or scpA do not. It is likely the attenuation observed in the sspA strain is due to polarity on the sspB gene.

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Section: Discussionmentioning

confidence: 99%

The role and regulation of the extracellular proteases of Staphylococcus aureus

et al. 2004

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“…Cleavage occurred between Ser 197 and Leu 198 , or between Ala 199 and Val 200 within the SLAVA motif and was inhibited by EDTA and o-phenanthroline. The metalloprotease of S. aureus is known to cleave at the Nterminal side of hydrophobic residues including leucine and valine (43) and is inhibited by EDTA and o-phenanthroline. It is produced throughout the growth cycle, in contrast to the other staphylococcal proteases, which are expressed predominantly in stationary phase (21,22).…”

Section: Discussionmentioning

confidence: 99%

Loss of Clumping Factor B Fibrinogen Binding Activity byStaphylococcus aureus Involves Cessation of Transcription, Shedding and Cleavage by Metalloprotease

McAleese

Walsh

Sieprawska

et al. 2001

Journal of Biological Chemistry

138

134

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The fibrinogen-binding protein clumping factor B (ClfB) of Staphylococcus aureus is present on the surface of cells from the early exponential phase of growth in greater amounts than on cells from late exponential phase and is barely detectable on cells from stationary phase. Expression of a clfB-lacZ fusion indicated that transcription stopped before the end of exponential phase. Mutations in the global regulators agr and sar had no effect on clfB transcription. The loss of ClfB protein from cells in stationary phase was due to expression ending before cells stopped growing, combined with shedding of some of the protein into the growth medium and dilution of those molecules remaining on the cell surface during the two to three cell division events leading to stationary phase. Two forms of the protein occurred on the cell surface, the smaller of which was generated by loss of a domain from the N terminus. The proportion of the smaller form increased as the cultures grew. The metalloprotease aureolysin was shown to be responsible for cleavage of ClfB. Cleav

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“…At least three different extracellular proteolytic enzymes are produced by Staphylococcus aureus (Arvidson et al, 1972(Arvidson et al, ,1973Arvidson, 1973a;Bjorklind & Jornvall, 1974;Houmard & Drapeau, 1972). One of these enzymes (proteinase I), which is a serine-proteinase (Dugas & Gaudet, 1975), cleaves peptide bonds only at the carboxyl terminal side of glutamic acid and aspartic acid.…”

Section: Introductionmentioning

confidence: 99%

“…Extracellular proteinases are thought generally to hydrolyse extracellular proteins to provide some of the amino acid requirement of the bacteria. This may not be the prime function of proteinase I, since peptides derived through hydrolysis of proteins by this enzyme are generally too large to be transported across the bacterial cell membrane (Payne & Gilvarg, 1971) unless other proteinases are produced (proteinase I1 and 111) (Arvidson, 1973 b ;Bjorklind & Jornvall, 1974). In order to understand the physiological role of proteinase I, we have investigated the regulation of the synthesis of this enzyme.…”

Section: Introductionmentioning

confidence: 99%

Influence of Amino Acids on the Synthesis of an Extracellular Proteinase from Staphylococcus aureus

Björklind

Arvidson

1978

Journal of General Microbiology

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The influence of amino acids on the synthesis of staphylococcal serine-proteinase (proteinase I) by Staphylococcus aureus strain v8 was studied. The repression of proteinase synthesis during the exponential growth phase was not due to any single amino acid in the medium. Proline was essential for proteinase synthesis in post-exponential growth but not for bacterial growth. At low concentrations of glycine, serine, threonine and proline, proteinase synthesis was inhibited, whereas at high concentrations of any of these amino acids, proteinase synthesis was fully induced. During post-exponential growth in the absence of glycine, serine, threonine or proline, the intracellular concentrations of alanine, aspartic acid and glutamic acid increased two to threefold. In the presence of these amino acids, the pool of alanine and aspartic acid remained at a low level and the concentration of glutamic acid decreased. The synthesis of proteinase I is probably repressed at high intracellular concentrations of glutamic acid.

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Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus

Cited by 41 publications

References 20 publications

The role and regulation of the extracellular proteases of Staphylococcus aureus

The role and regulation of the extracellular proteases of Staphylococcus aureus

Loss of Clumping Factor B Fibrinogen Binding Activity byStaphylococcus aureus Involves Cessation of Transcription, Shedding and Cleavage by Metalloprotease

Influence of Amino Acids on the Synthesis of an Extracellular Proteinase from Staphylococcus aureus

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