A Method for Structure-Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
Date
2009-12
Authors
Tian, XiaoLin
Syvitski, Raymond T.
Liu, TianLei
Livingstone, Nadine
Jakeman, David L.
Li, Yung-Hua
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Abstract
Many species of streptococci secrete and use a competence-stimulating peptide (CSP) to initiate
quorum sensing for induction of genetic competence, bacteriocin production, and other activities.
These signaling molecules are small, unmodified peptides that induce powerful strain-specific
activity at nano-molar concentrations. This feature has provided an excellent opportunity to explore
their structure-function relationships. However, CSP variants have also been identified in many
species, and each specifically activates its cognate receptor. How such minor changes dramatically
affect the specificity of these peptides remains unclear. Structure-activity analysis of these
peptides may provide clues for understanding the specificity of signaling peptide-receptor
interactions. Here, we use the Streptococcus mutans CSP as an example to describe methods of
analyzing its structure-activity relationship. The methods described here may provide a platform for
studying quorum-sensing signaling peptides of other naturally transformable streptococci.
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Citation
Tian, XiaoLin, Raymond T. Syvitski, TianLei Liu, Nadine Livingstone, et al. 2009. "A Method for Structure-Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally
Transformable Streptococci." Biological Procedures Online 11(1): 207-226.