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Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
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Related Experiment Video

Updated: May 11, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Enterolyin S, a Polythiazole-containing Hemolytic Peptide from Enterococcus caccae.

Chengyou Shi1,2, Varshal A Patel3, Douglas A Mitchell1,4

  • 1Carl R. Woese Institute for Genomic Biology, University of Illinois, Urbana Champaign, Urbana, IL, 61801, USA.

Chembiochem : a European Journal of Chemical Biology
|April 22, 2024
PubMed
Summary

Researchers discovered enterolysin S (ELS), a hemolytic peptide from Enterococcus caccae, structurally similar to streptolysin S (SLS). This finding expands the known family of virulence-promoting linear azol(in)e-containing peptides (LAPs).

Keywords:
LAPRiPPsYcaOcytolysinpeptidepost-translational modificationstreptolysin Sthiazolevirulence factor

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Streptolysin S (SLS) is a key virulence factor in Streptococcus pyogenes, but its structure remains elusive due to challenging physicochemical properties.
  • Linear azol(in)e-containing peptides (LAPs) are a class of modified peptides with significant roles in microbial virulence.

Purpose of the Study:

  • To discover and characterize novel hemolytic peptides analogous to SLS.
  • To expand the understanding of LAP structures and their contribution to virulence.

Main Methods:

  • Heterologous expression of a novel peptide from Enterococcus caccae.
  • Site-directed mutagenesis and chemoselective modification.
  • High-resolution mass spectrometry for structural elucidation.

Main Results:

  • Discovery and characterization of enterolysin S (ELS), a hemolytic peptide from E. caccae.
  • ELS was found to contain a contiguous octathiazole moiety.
  • ELS represents a new member of the hemolytic LAP family.

Conclusions:

  • Enterolysin S (ELS) is a novel hemolytic LAP, expanding the known diversity of these virulence factors.
  • The structural characterization of ELS provides new insights into the LAP family.
  • This discovery aids in understanding bacterial virulence mechanisms.