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Structure of the pheromone peptide of the Staphylococcus epidermidis agr system
Author(s) -
Otto Michael,
Süßmuth Roderich,
Jung Günther,
Götz Friedrich
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00145-8
Subject(s) - staphylococcus epidermidis , peptide , quorum sensing , pheromone , biological activity , virulence , chemistry , cysteine , biochemistry , extracellular , biology , microbiology and biotechnology , staphylococcus aureus , bacteria , enzyme , gene , genetics , in vitro
The agr quorum‐sensing system is responsible for the regulation of several virulence factors in staphylococci, with an extracellular pheromone peptide as signalling molecule. By monitoring the biological activity of synthetic peptides, it could be demonstrated that the pheromone of the agr system in Staphylococcus epidermidis is an octapeptide containing a thiolester linkage between the central cysteine and the C‐terminal carboxyl group. The peptide was active at nanomolar concentrations. The N‐terminus of the peptide pheromone, which is encoded as part of a protein precursor, proved to be crucial for biological activity.