Extracellular proteins of Staphylococcus aureus and the role of SarA and B

Ziebandt, Anne-Kathrin; Weber, H.W.; Rudolph, Jens; Schmid, Roland M.; Höper, Dirk W.; Engelmann, Susanne; Hecker, Michael

doi:10.1002/1615-9861(200104)1:4<480::aid-prot480>3.3.co;2-f

Cited by 86 publications

(151 citation statements)

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“…Pathogenesis of S. aureus involves the synthesis of cell wall-associated virulence factors, a large number of extracellular proteins, and secreted toxins with damaging effects on the host cells. To identify extracellular proteins of S. aureus that are potential virulence factors, Ziebandt et al (162) used a proteomic approach to analyze the pattern of extracellular proteins of different S. aureus strains. In total, 26 proteins of the approximately 100 protein spots could be identified.…”

Section: Staphylococcus Aureusmentioning

confidence: 99%

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Tjalsma¹,

Antelmann

Jongbloed³

et al. 2004

Microbiol Mol Biol Rev

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513

519

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SUMMARY Secretory proteins perform a variety of important“ remote-control” functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make predictions about the composition of bacterial machinery for protein secretion as well as the extracellular complement of bacterial proteomes. Recently, the power of proteomics was successfully employed to evaluate genome-based models of these so-called secretomes. Progress in this field is well illustrated by the proteomic analysis of protein secretion by the gram-positive bacterium Bacillus subtilis, for which ∼90 extracellular proteins were identified. Analysis of these proteins disclosed various“ secrets of the secretome,” such as the residence of cytoplasmic and predicted cell envelope proteins in the extracellular proteome. This showed that genome-based predictions reflect only∼ 50% of the actual composition of the extracellular proteome of B. subtilis. Importantly, proteomics allowed the first verification of the impact of individual secretion machinery components on the total flow of proteins from the cytoplasm to the extracellular environment. In conclusion, proteomics has yielded a variety of novel leads for the analysis of protein traffic in B. subtilis and other gram-positive bacteria. Ultimately, such leads will serve to increase our understanding of virulence factor biogenesis in gram-positive pathogens, which is likely to be of high medical relevance.

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Section: Staphylococcus Aureusmentioning

confidence: 99%

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Tjalsma¹,

Antelmann

Jongbloed³

et al. 2004

Microbiol Mol Biol Rev

Self Cite

513

519

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“…Proteomics-based data sets of membrane, cell wall, and extracellular proteins were extremely valuable for a recent verification of signal peptide predictions for B. subtilis (179). Such data sets are now becoming available for S. aureus, as exemplified by studies on the membrane and cell wall proteomes of S. aureus Phillips (127) and the extracellular proteomes of S. aureus strains derived from the recently sequenced NCTC8325 and COL strains (208,209) (Fig. 2).…”

Section: Signal Peptide Predictionsmentioning

confidence: 99%

Mapping the Pathways to StaphylococcalPathogenesis by Comparative Secretomics

Sibbald

Ziebandt

Engelmann

et al. 2006

Microbiol Mol Biol Rev

231

304

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SUMMARY The gram-positive bacterium Staphylococcus aureus is a frequent component of the human microbial flora that can turn into a dangerous pathogen. As such, this organism is capable of infecting almost every tissue and organ system in the human body. It does so by actively exporting a variety of virulence factors to the cell surface and extracellular milieu. Upon reaching their respective destinations, these virulence factors have pivotal roles in the colonization and subversion of the human host. It is therefore of major importance to obtain a clear understanding of the protein transport pathways that are active in S. aureus. The present review aims to provide a state-of-the-art roadmap of staphylococcal secretomes, which include both protein transport pathways and the extracytoplasmic proteins of these organisms. Specifically, an overview is presented of the exported virulence factors, pathways for protein transport, signals for cellular protein retention or secretion, and the exoproteomes of different S. aureus isolates. The focus is on S. aureus, but comparisons with Staphylococcus epidermidis and other gram-positive bacteria, such as Bacillus subtilis, are included where appropriate. Importantly, the results of genomic and proteomic studies on S. aureus secretomes are integrated through a comparative “secretomics” approach, resulting in the first definition of the core and variant secretomes of this bacterium. While the core secretome seems to be largely employed for general housekeeping functions which are necessary to thrive in particular niches provided by the human host, the variant secretome seems to contain the “gadgets” that S. aureus needs to conquer these well-protected niches.

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“…The specific mechanism by which Aur maturation occurs is unknown; however, it is common amongst the thermolysin-like enzymes for this to be achieved via auto-catalysis (Miyoshi & Shinoda, 2000). Little is known about staphopain; it too is produced in zymogen form and must undergo proteolytic cleavage to attain activity (Arvidson, 2000;Hofmann et al, 1993;Ziebandt et al, 2001). …”

Section: Introductionmentioning

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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Extracellular proteins of Staphylococcus aureus and the role of SarA and B

Cited by 86 publications

References 0 publications

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Mapping the Pathways to StaphylococcalPathogenesis by Comparative Secretomics

The role and regulation of the extracellular proteases of Staphylococcus aureus

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