The leaderless communication peptide (LCP) class of quorum-sensing peptides is broadly distributed among Firmicutes

Shifu Aggarwal; Elaine Huang; Hackwon Do; Nishanth Makthal; Yanyan Li; Eric Bapteste; Philippe Lopez; Charles Bernard; Muthiah Kumaraswami

doi:10.1038/s41467-023-41719-3

The leaderless communication peptide (LCP) class of quorum-sensing peptides is broadly distributed among Firmicutes

Shifu Aggarwal, Elaine Huang, Hackwon Do, Nishanth Makthal, Yanyan Li, Eric Bapteste, Philippe Lopez, Charles Bernard, Muthiah Kumaraswami

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The human pathogen Streptococcus pyogenes secretes a short peptide (leaderless communication peptide, LCP) that mediates intercellular communication and controls bacterial virulence through interaction with its receptor, RopB. Here, we show that LCP and RopB homologues are present in other Firmicutes. We experimentally validate that LCPs with distinct peptide communication codes act as bacterial intercellular signals and regulate gene expression in Streptococcus salivarius, Streptococcus porcinus, Enterococcus malodoratus and Limosilactobacillus reuteri. Our results indicate that LCPs are more widespread than previously thought, and their characterization may uncover new signaling mechanisms and roles in coordinating diverse bacterial traits.

Original language	English (US)
Article number	5947
Pages (from-to)	5947
Journal	Nature Communications
Volume	14
Issue number	1
DOIs	https://doi.org/10.1038/s41467-023-41719-3
State	Published - Sep 23 2023

Keywords

Humans
Firmicutes
Quorum Sensing
Cell Communication
Peptides
Phenotype

ASJC Scopus subject areas

Physics and Astronomy(all)
Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)

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10.1038/s41467-023-41719-3

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title = "The leaderless communication peptide (LCP) class of quorum-sensing peptides is broadly distributed among Firmicutes",

abstract = "The human pathogen Streptococcus pyogenes secretes a short peptide (leaderless communication peptide, LCP) that mediates intercellular communication and controls bacterial virulence through interaction with its receptor, RopB. Here, we show that LCP and RopB homologues are present in other Firmicutes. We experimentally validate that LCPs with distinct peptide communication codes act as bacterial intercellular signals and regulate gene expression in Streptococcus salivarius, Streptococcus porcinus, Enterococcus malodoratus and Limosilactobacillus reuteri. Our results indicate that LCPs are more widespread than previously thought, and their characterization may uncover new signaling mechanisms and roles in coordinating diverse bacterial traits.",

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author = "Shifu Aggarwal and Elaine Huang and Hackwon Do and Nishanth Makthal and Yanyan Li and Eric Bapteste and Philippe Lopez and Charles Bernard and Muthiah Kumaraswami",

note = "Funding Information: This work was supported in part by the National Institutes of Health grants R01 AI146048 and R01AI162748 to M.K. We thank Carmen Tartera for providing S. salivarius strain. Publisher Copyright: {\textcopyright} 2023, Springer Nature Limited.",

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AU - Aggarwal, Shifu

AU - Huang, Elaine

AU - Do, Hackwon

AU - Makthal, Nishanth

AU - Li, Yanyan

AU - Bapteste, Eric

AU - Lopez, Philippe

AU - Bernard, Charles

AU - Kumaraswami, Muthiah

N1 - Funding Information: This work was supported in part by the National Institutes of Health grants R01 AI146048 and R01AI162748 to M.K. We thank Carmen Tartera for providing S. salivarius strain. Publisher Copyright: © 2023, Springer Nature Limited.

PY - 2023/9/23

Y1 - 2023/9/23

N2 - The human pathogen Streptococcus pyogenes secretes a short peptide (leaderless communication peptide, LCP) that mediates intercellular communication and controls bacterial virulence through interaction with its receptor, RopB. Here, we show that LCP and RopB homologues are present in other Firmicutes. We experimentally validate that LCPs with distinct peptide communication codes act as bacterial intercellular signals and regulate gene expression in Streptococcus salivarius, Streptococcus porcinus, Enterococcus malodoratus and Limosilactobacillus reuteri. Our results indicate that LCPs are more widespread than previously thought, and their characterization may uncover new signaling mechanisms and roles in coordinating diverse bacterial traits.

AB - The human pathogen Streptococcus pyogenes secretes a short peptide (leaderless communication peptide, LCP) that mediates intercellular communication and controls bacterial virulence through interaction with its receptor, RopB. Here, we show that LCP and RopB homologues are present in other Firmicutes. We experimentally validate that LCPs with distinct peptide communication codes act as bacterial intercellular signals and regulate gene expression in Streptococcus salivarius, Streptococcus porcinus, Enterococcus malodoratus and Limosilactobacillus reuteri. Our results indicate that LCPs are more widespread than previously thought, and their characterization may uncover new signaling mechanisms and roles in coordinating diverse bacterial traits.

KW - Humans

KW - Firmicutes

KW - Quorum Sensing

KW - Cell Communication

KW - Peptides

KW - Phenotype

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The leaderless communication peptide (LCP) class of quorum-sensing peptides is broadly distributed among Firmicutes

Abstract

Keywords

ASJC Scopus subject areas

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