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CylA is a sequence-specific protease involved in toxin biosynthesis.

Weixin Tang1, Silvia C Bobeica1, Li Wang2

  • 1Department of Chemistry, Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, IL, 61801, USA.

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The enterococcal cytolysin (CylA) protease self-activates and cleaves leader peptides for lantibiotic maturation. This serine protease is a valuable tool for discovering new lanthipeptides and developing therapies against enterococcal infections.

Keywords:
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Area of Science:

  • Biochemistry
  • Microbiology
  • Molecular Biology

Background:

  • CylA is a subtilisin-like serine protease involved in enterococcal cytolysin biosynthesis.
  • Enterococcal cytolysin is a lantibiotic crucial for virulence in *Enterococcus faecalis* infections.

Purpose of the Study:

  • To characterize the enzymatic activity and substrate specificity of CylA.
  • To explore the potential of CylA as a tool for lanthipeptide discovery and therapeutic development.

Main Methods:

  • In vitro reconstitution assays using purified CylA.
  • Analysis of peptide cleavage specificity with linear and modified substrates.
  • Biochemical characterization of CylA self-activation.

Main Results:

  • CylA self-activates by cleaving its N-terminal 95 amino acids.
  • The protease exhibits sequence-specific, traceless cleavage of leader peptides, accepting both linear and modified substrates with a preference for cyclized forms.
  • CylA demonstrates broad applicability for leader peptide removal from various post-translationally modified peptides.

Conclusions:

  • CylA is a versatile leader peptidase with significant potential for mining novel lanthipeptides.
  • Understanding CylA's substrate specificity can inform the development of protease inhibitors to combat enterococcal infections.