2010
DOI: 10.1096/fj.09-145631
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Streptococcus pyogenesSpyCEP: a chemokine‐inactivating protease with unique structural and biochemical features

Abstract: SpyCEP is a 170-kDa multidomain serine protease expressed on the surface of the human pathogen Streptococcus pyogenes, which plays an important role in infection by catalyzing cleavage and inactivation of the neutrophil chemoattractant interleukin-8. In this study, we investigated the biochemical features and maturation process of SpyCEP, starting from a recombinant form of the protease expressed and purified from Escherichia coli. We show that active recombinant SpyCEP differs from other bacterial proteases i… Show more

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Cited by 49 publications
(68 citation statements)
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References 27 publications
(35 reference statements)
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“…The stability of SpyCEP , and the relative instability of the SpyCEP 113-244 domain, have been described previously (Zingaretti et al, 2010). Here, a new construct, SpyCEP 245-1131 , lacking $500 Cterminal residues, was prepared.…”
Section: Resultsmentioning
confidence: 88%
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“…The stability of SpyCEP , and the relative instability of the SpyCEP 113-244 domain, have been described previously (Zingaretti et al, 2010). Here, a new construct, SpyCEP 245-1131 , lacking $500 Cterminal residues, was prepared.…”
Section: Resultsmentioning
confidence: 88%
“…Using PIPE PCR cloning (Klock & Lesley, 2009) and the GAS M1 strain SpyCEP ectodomain (residues 34-1613; UniProt Q9A180) in pET-21b (Zingaretti et al, 2010), three SpyCEP constructs were prepared in pET-28a, termed SpyCEP 113-244 , SpyCEP 245-1131 and SpyCEP (Fig. 1a), excluding residues 33-112 because of predicted disorder and excluding residues 1132 onwards in order to mimic the C5a peptidase construct used for structure determination (Kagawa et al, 2009).…”
Section: Cloning Expression and Purification Of Spycep Proteinsmentioning
confidence: 99%
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