Structural and functional features of Streptolysin O

Int J Bioinform Res Appl. 2011;7(4):427-44. doi: 10.1504/IJBRA.2011.043772.

Abstract

Streptolysin O, a 63 kDa exotoxin coded by slo gene, is a well-characterised thiol-activated cytolysin, which damages cholesterol-containing membranes resulting in disruption and lysis of the target cell. On the basis of homology model and secondary structure analysis, the toxin has four domains of which domain 4 is of particular importance and is directly linked to domain 2 by a glycine linker and remained consistent in initial membrane recognition. Domain 4 reduces the hydrophobic ratio when compared with its template, which would affect the activity of the toxin at low pH.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Base Sequence
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Streptolysins / chemistry*

Substances

  • Bacterial Proteins
  • Streptolysins
  • streptolysin O