Genetic and Biochemical Properties of Streptococcal NAD-glycohydrolase Inhibitor

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Genetic and biochemical properties of streptococcal NAD-glycohydrolase inhibitor.

The gene encoding streptolysin O (slo), a cytolysin of hemolytic streptococci, is transcribed polycistronically from the promoter of the preceding NAD-glycohydrolase (NADase) gene (nga). Between nga and slo, a putative open reading frame (orf1) is located whose function has been totally unknown. Present investigation demonstrated that the orf1 encodes a protein designated as streptococcal NADas...

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A Novel Endogenous Inhibitor of the Secreted Streptococcal NAD-Glycohydrolase

The Streptococcus pyogenes NAD-glycohydrolase (SPN) is a toxic enzyme that is introduced into infected host cells by the cytolysin-mediated translocation pathway. However, how S. pyogenes protects itself from the self-toxicity of SPN had been unknown. In this report, we describe immunity factor for SPN (IFS), a novel endogenous inhibitor that is essential for SPN expression. A small protein of ...

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Inhibition of Inflammasome-Dependent Interleukin 1β Production by Streptococcal NAD+-Glycohydrolase: Evidence for Extracellular Activity

Group A Streptococcus (GAS) is a common human pathogen and the etiologic agent of a large number of diseases ranging from mild, self-limiting infections to invasive life-threatening conditions. Two prominent virulence factors of this bacterium are the genetically and functionally linked pore-forming toxin streptolysin O (SLO) and its cotoxin NAD+-glycohydrolase (NADase). Overexpression of these...

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Identity of Streptolysin - 0 and NAD - Glycohydrolase

The homogeneity of purified NAD-glycohydrolase (EC 3.2.2.5) from Group C streptococci was demonstrated by analytical ultracentrifugation, disc electrophoresis and immunochemical analysis. Together with earlier characterization procedures the data show that the enzyme is homogenous in molecular seize, molecular form and electrophoretic charge. In addition, the enzyme has been shown to possess st...

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Purification of NAD+ glycohydrolase from human serum

In the present study, NAD+ glycohydrolase was purified from serum samples collected from healthy individuals using ammonium sulfate fractionation, Affi-Gel blue (Cibacron Blue F3GA) affinity chromatography, Sephadex G-100 column chromatography and isoelectric focusing. The final step was followed by a second Sephadex G-100 column chromatography assay in order to remove the ampholytes from the i...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2006

ISSN: 0021-9258

DOI: 10.1074/jbc.m506879200