Processing, stability, and kinetic parameters of C5a peptidase fromStreptococcus pyogenes
نویسندگان
چکیده
منابع مشابه
Complete nucleotide sequence of the streptococcal C5a peptidase gene of Streptococcus pyogenes.
Streptococcal C5a peptidase (SCP), a recently discovered virulence factor of Streptococcus pyogenes, specifically cleaves the human serum chemotaxin C5a near its carboxyl terminus, destroying its ability to serve as a chemoattractant. We previously localized the SCP gene, scpA, to the 5.8-kb insert of the recombinant plasmid pTT1. Here we present the complete nucleotide sequence of scpA and its...
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Resistance to phagocytosis is a hallmark of virulent Streptococcus pyogenes (group A streptococcus). Surface-bound C5a peptidase reduces recruitment of phagocytes to the site of infection, and hyaluronic acid capsules and/or the M protein limit the uptake of streptococci. In this study the relative impact of M and M-like proteins and the C5a peptidase on the virulence of a serotype M49 strain w...
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A glutathione-S-transferase (GST)-C5a-green fluorescent protein (GFP) fusion protein was designed for use as a substrate for the streptococcal C5a peptidase (SCPA). The substrate was immobilized on a glutathione-Sepharose affinity matrix and used to measure wild-type SCPA activity in the range of 0.8 to 800 nM. The results of the assay demonstrated that SCPA is highly heat stable and has optima...
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Subunit 9 (dicyclohexylcarbodiimide binding protein, ‘proteolipid’) of the mitochondrial F lFo-ATPase is a nuclearly coded protein in Neurospora crassa. It is synthesized on free cytoplasmic ribosomes as a larger precursor with an NH2-terminal peptide extension. The peptide extension is cleaved off after transport of the protein into the mitochondria. A processing activity referred to as proces...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2002
ISSN: 0014-2956
DOI: 10.1046/j.1432-1033.2002.03183.x