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
DOIs
StatePublished - 1995

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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