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Biological activity and identification of a peptide inhibitor of LuxS from Streptococcus suis serotype 2.
- Source :
-
FEMS microbiology letters [FEMS Microbiol Lett] 2009 May; Vol. 294 (1), pp. 16-23. Date of Electronic Publication: 2008 Mar 18. - Publication Year :
- 2009
-
Abstract
- The virulence of bacterial communities may be regulated by mechanisms involving the synthesis of the quorum-sensing signal autoinducer 2 (AI-2), which allows both intra- and interspecies communication. AI-2 is produced in bacteria that express the gene luxS. In the present study, expressed and purified LuxS from Streptococcus suis serotype 2 (SS2) was used to catalyze the substrate S-ribosylhomocysteine in a reaction that leads to the production of AI-2. The biological activity of the in vitro synthesized AI-2 was demonstrated in a Vibrio harveyi strain BB170 bioassay; real-time PCR results showed that biosynthesis of AI-2 can increase the virulence of SS2. Phage-encoded peptides that specifically interact with the LuxS enzyme were selected following three rounds of phage display. One such peptide inhibitor (TNRHNPHHLHHV) of LuxS was shown to partially inhibit the activity of the enzyme. Furthermore, 14 peptides containing the consensus sequence HSIR showed high affinity with LuxS. The selected and characterized specific inhibitor as well as the high-affinity ligands may facilitate the identification of new vaccination targets, opening up new approaches to the development of therapeutic drugs.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins isolation & purification
Biological Assay
Carbon-Sulfur Lyases isolation & purification
Enzyme Inhibitors isolation & purification
Gene Expression Profiling
Homocysteine analogs & derivatives
Homocysteine metabolism
Homoserine analogs & derivatives
Homoserine metabolism
Humans
Lactones metabolism
Molecular Sequence Data
Peptide Library
Peptides isolation & purification
Quorum Sensing
Reverse Transcriptase Polymerase Chain Reaction
Streptococcus suis pathogenicity
Vibrio physiology
Virulence Factors biosynthesis
Bacterial Proteins antagonists & inhibitors
Carbon-Sulfur Lyases antagonists & inhibitors
Enzyme Inhibitors pharmacology
Peptides pharmacology
Streptococcus suis enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1574-6968
- Volume :
- 294
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- FEMS microbiology letters
- Publication Type :
- Academic Journal
- Accession number :
- 19493004
- Full Text :
- https://doi.org/10.1111/j.1574-6968.2009.01534.x