A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci

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...

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Main Authors:	Tian, XiaoLin, Syvitski, Raymond T, Liu, TianLei, Livingstone, Nadine, Jakeman, David L, Li, Yung-Hua
Format:	Online
Language:	English
Published:	BioMed Central 2009
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3055912/

id	pubmed-3055912
recordtype	oai_dc
spelling	pubmed-30559122011-03-12 A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci Tian, XiaoLin Syvitski, Raymond T Liu, TianLei Livingstone, Nadine Jakeman, David L Li, Yung-Hua Methodology 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. BioMed Central 2009-06-11 /pmc/articles/PMC3055912/ /pubmed/19517207 http://dx.doi.org/10.1007/s12575-009-9009-9 Text en Copyright ©2009 Tian et al. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Tian, XiaoLin Syvitski, Raymond T Liu, TianLei Livingstone, Nadine Jakeman, David L Li, Yung-Hua
spellingShingle	Tian, XiaoLin Syvitski, Raymond T Liu, TianLei Livingstone, Nadine Jakeman, David L Li, Yung-Hua A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
author_facet	Tian, XiaoLin Syvitski, Raymond T Liu, TianLei Livingstone, Nadine Jakeman, David L Li, Yung-Hua
author_sort	Tian, XiaoLin
title	A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
title_short	A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
title_full	A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
title_fullStr	A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
title_full_unstemmed	A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci
title_sort	method for structure–activity analysis of quorum-sensing signaling peptides from naturally transformable streptococci
description	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.
publisher	BioMed Central
publishDate	2009
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3055912/
_version_	1611445247059951616

A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci

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