Different forms of Streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin: Cleavage by streptococcal cysteine protease

M. Pinkney, V. Kapur, J. Smith, U. Weller, M. Palmer, M. Glanville, M. Messner, J. M. Musser, S. Bhakdi, M. A. Kehoe

Research output: Contribution to journalArticle

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Abstract

To resolve apparent discrepancies in the literature, N-terminal sequences of the active high- and low-molecular-weight (high- and low-M(r)) forms of native streptolysin O (nSLO) purified from Streptococcus pyogenes culture supernatants and of the similar-size high- and low-M(r) forms of recombinant SLO (rSLO) found in the periplasm of Escherichia coli expressing a cloned slo gene were determined. The high-M(r) forms of nSLO and rSLO are identical, reflecting removal of a 31-residue signal peptide, but the similar-size low- M(r) forms are very different. Removal of C-terminal sequences by proteases in the E. coli periplasm produces an inactive low-M(r) form of rSLO. In contrast, an active low-M(r) form of nSLO is produced by proteolytic cleavage between the N-terminal residues Lys-77 and Leu-78, which was shown to correspond to an extremely sensitive cleavage site for the pyrogenic exotoxin B-derived streptococcal cysteine protease.

Original languageEnglish (US)
Pages (from-to)2776-2779
Number of pages4
JournalInfection and Immunity
Volume63
Issue number7
StatePublished - Jan 1 1995

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Cysteine Proteases
Streptococcus pyogenes
Periplasm
Escherichia coli
Protein Sorting Signals
Molecular Weight
Genes
streptolysin O

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

Pinkney, M. ; Kapur, V. ; Smith, J. ; Weller, U. ; Palmer, M. ; Glanville, M. ; Messner, M. ; Musser, J. M. ; Bhakdi, S. ; Kehoe, M. A. / Different forms of Streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin : Cleavage by streptococcal cysteine protease. In: Infection and Immunity. 1995 ; Vol. 63, No. 7. pp. 2776-2779.
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Pinkney, M, Kapur, V, Smith, J, Weller, U, Palmer, M, Glanville, M, Messner, M, Musser, JM, Bhakdi, S & Kehoe, MA 1995, 'Different forms of Streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin: Cleavage by streptococcal cysteine protease', Infection and Immunity, vol. 63, no. 7, pp. 2776-2779.

Different forms of Streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin : Cleavage by streptococcal cysteine protease. / Pinkney, M.; Kapur, V.; Smith, J.; Weller, U.; Palmer, M.; Glanville, M.; Messner, M.; Musser, J. M.; Bhakdi, S.; Kehoe, M. A.

In: Infection and Immunity, Vol. 63, No. 7, 01.01.1995, p. 2776-2779.

Research output: Contribution to journalArticle

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T1 - Different forms of Streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin

T2 - Cleavage by streptococcal cysteine protease

AU - Pinkney, M.

AU - Kapur, V.

AU - Smith, J.

AU - Weller, U.

AU - Palmer, M.

AU - Glanville, M.

AU - Messner, M.

AU - Musser, J. M.

AU - Bhakdi, S.

AU - Kehoe, M. A.

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Y1 - 1995/1/1

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AB - To resolve apparent discrepancies in the literature, N-terminal sequences of the active high- and low-molecular-weight (high- and low-M(r)) forms of native streptolysin O (nSLO) purified from Streptococcus pyogenes culture supernatants and of the similar-size high- and low-M(r) forms of recombinant SLO (rSLO) found in the periplasm of Escherichia coli expressing a cloned slo gene were determined. The high-M(r) forms of nSLO and rSLO are identical, reflecting removal of a 31-residue signal peptide, but the similar-size low- M(r) forms are very different. Removal of C-terminal sequences by proteases in the E. coli periplasm produces an inactive low-M(r) form of rSLO. In contrast, an active low-M(r) form of nSLO is produced by proteolytic cleavage between the N-terminal residues Lys-77 and Leu-78, which was shown to correspond to an extremely sensitive cleavage site for the pyrogenic exotoxin B-derived streptococcal cysteine protease.

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