Editor: Robert Gunsalus
Biological activity and identification of a peptide inhibitor of LuxS from Streptococcus suis serotype 2
Article first published online: 18 MAR 2009
© 2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved
FEMS Microbiology Letters
Volume 294, Issue 1, pages 16–23, May 2009
How to Cite
Han, X. and Lu, C. (2009), Biological activity and identification of a peptide inhibitor of LuxS from Streptococcus suis serotype 2. FEMS Microbiology Letters, 294: 16–23. doi: 10.1111/j.1574-6968.2009.01534.x
- Issue published online: 2 APR 2009
- Article first published online: 18 MAR 2009
- Received 4 August 2008; accepted 24 January 2009.First published online 18 March 2009.
- Streptococcus suis serotype 2;
- phage display
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.