The epidermolytic (exfoliative) toxins of Staphylococcus aureus

Bailey, Christopher J.; Lockhart, Brian P.; Redpath, Maria B.; Smith, Thomas P.

doi:10.1007/bf00221387

Cited by 31 publications

(30 citation statements)

References 56 publications

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“…Members of the serine protease family, including V8 protease and the ETs, contain a well-conserved active site, known as a catalytic triad (4,10,11). This motif is characterized by the presence of a highly reactive serine residue within hydrogen-bonding distance of an imidazole ring nitrogen of histidine and a transition state-stabilizing aspartate residue (6,14).…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of a NovelStaphylococcus aureusSerine Protease Operon

et al. 2001

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The present study identified and characterized a unique operon (spl) encoding six serine protease-like proteins. In addition, native Spl proteins were isolated and characterized. Typical of most exoproteins, the spl gene products contain putative 35-or 36-amino-acid signal peptides. The Spl proteins share 44 to 95% amino acid sequence identity with each other and 33 to 36% sequence identity with V8 protease. They also contain amino acids found in catalytic triads of enzymes in the trypsin-like serine protease family, and SplB and SplC were shown to degrade casein. The spl operon is transcribed on a 5.5-kb transcript, but several nonrandom degradation products of this transcript were also identified. Similar to other S. aureus exoprotein genes, the spl operon is maximally expressed during the transition into stationary phase and is positively controlled by the Agr virulence factor regulator. The Sar regulatory system did not affect spl operon expression. PCR analysis revealed the presence of the spl operon in 64% of the S. aureus isolates tested, although one spl operon-negative isolate was shown to contain at least two of the spl genes. Finally, intraperitoneal injection of an spl operon deletion mutant revealed no major differences in virulence compared to the parental strain.Staphylococcus aureus exports a wide variety of exoenzymes, some of which are known virulence factors. Among these enzymes are a variety of proteases, such as metalloprotease, thiolprotease, and the serine proteases V8 and exfoliative toxin A (ETA) and ETB. The best characterized of these, V8 serine protease, was initially isolated from S. aureus strain V8 but has since been shown to be expressed by 67% of the S. aureus isolates tested (2, 11).Like most exoproteins produced by S. aureus, the Agr regulatory system positively regulates extracellular protease expression in response to increasing cell density (7,26). In contrast, the Sar regulatory system has a negative effect on protease expression. Recent studies indicate that pleiotropic alterations in exoprotein profiles caused by sar mutations are due to the derepression of staphylococcal proteases, which then leads to exoprotein degradation (7, 9). In addition, McGavin et al. (21) reported that V8 protease modifies the fibronectin-binding phenotype of S. aureus. Thus, secreted proteases could play an important role in the posttranslational regulation of S. aureus exoprotein activity, in addition to modifying host proteins to the benefit of the bacteria.In this study, we identified a novel S. aureus operon (designated spl) that encodes six previously uncharacterized serine protease-like proteins. This operon is expressed during the transition to stationary phase and is positively regulated by Agr. In addition, two of the Spl proteins expressed by this operon were shown to exhibit proteolytic activity. MATERIALS AND METHODSBacterial strains and plasmids. The bacterial strains and plasmids used in this study are listed in Table 1. S. aureus strains were routinely grown in tryptic soy broth...

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Section: Discussionmentioning

confidence: 99%

Molecular Characterization of a NovelStaphylococcus aureusSerine Protease Operon

et al. 2001

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“…This discussion will focus on the exfoliative toxins of S. aureus and the mechanism by which they cause disease in humans. but not in rats, rabbits, dogs, hedgehogs, voles, guinea pigs, chickens or frogs (Bailey et al, 1995;Elias et al, 1975;Ladhani et al, 1999).…”

Section: Introductionmentioning

confidence: 94%

Staphylococcus aureus exfoliative toxins: How they cause disease.

Plano¹

2004

Journal of Investigative Dermatology

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“…116 Additionally, other mutations have been identified in patients who have monilethrix hairs as a part of their phenotypic presentation -monilethrix-like congenital hypotrichosis. 110,118 infectious diseases targeting the desmosome Recent research has shown that the desmosome can be targeted during infection. Specifically, the discovery that staphylococcal exfoliative toxins (ETs) can cleave a desmosomal cadherin has shed light on the pathophysiology of a number of blistering diseases with common infective etiology.…”

Section: Desmogleinmentioning

confidence: 99%

Desmosome assembly, homeostasis, and desmosomal disease

Cirillo¹

2016

CHC

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Cell-cell adhesion is involved in all aspects of tissue behavior in multicellular organisms, from tissue morphogenesis (regulation of cell shape, apoptosis, cell movement, and development of complex structures) to aging and disease. A major player in the dynamic regulation of intercellular contacts is the desmosome. Knowledge of the desmosome has evolved over 150 years from the notion of a static, punctuate, adhesive barrier structure to one of the finely tuned multifunctional complexes involved in the regulation of numerous and diverse aspects of keratinocyte physiology and disease. In this context, nondesmosomal regulatory molecules have been acquiring increasing importance in the study of desmosome homeostasis and have become part of the extended desmosomal interactome named "desmo-adhesome". Among these associated molecules, kinases are the prominent regulators of both desmosome remodeling and acquisition of hyperadhesion, two novel concepts in cell-cell adhesion. Spatiotemporal changes in the expression and regulation of desmosomal proteins also underlie a number of genetic, infectious, autoimmune, and malignant conditions. In addition to offering a systems-level view of the molecular composition of desmosomes, we also discuss the mechanisms that regulate, and disrupt, desmosome homeostasis.

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The epidermolytic (exfoliative) toxins of Staphylococcus aureus

Cited by 31 publications

References 56 publications

Molecular Characterization of a NovelStaphylococcus aureusSerine Protease Operon

Molecular Characterization of a NovelStaphylococcus aureusSerine Protease Operon

Staphylococcus aureus exfoliative toxins: How they cause disease.

Desmosome assembly, homeostasis, and desmosomal disease

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