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N-terminal ArgD peptides from the classical Staphylococcus aureus Agr system have cytotoxic and proinflammatory activities.


ABSTRACT: AgrD is the precursor for the autoinducing peptide in a quorum-sensing system regulating virulence phenotypes of the preeminent pathogen Staphylococcus aureus. Mass spectrometry-based methods, including molecular networking, identified formylated and nonformylated peptide variants derived from the AgrD N-terminal leader domain in S. aureus cell-free culture supernatants. Functional assessment of these peptides revealed unexpected bioactivities, including human cell-line cytotoxicity, modulation of neutrophil chemotaxis, neutrophil extracellular trap formation, and the aggravation of skin lesions in vivo.

SUBMITTER: Gonzalez DJ 

PROVIDER: S-EPMC4304878 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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N-terminal ArgD peptides from the classical Staphylococcus aureus Agr system have cytotoxic and proinflammatory activities.

Gonzalez David J DJ   Corriden Ross R   Akong-Moore Kathryn K   Olson Joshua J   Dorrestein Pieter C PC   Nizet Victor V  

Chemistry & biology 20141101 11


AgrD is the precursor for the autoinducing peptide in a quorum-sensing system regulating virulence phenotypes of the preeminent pathogen Staphylococcus aureus. Mass spectrometry-based methods, including molecular networking, identified formylated and nonformylated peptide variants derived from the AgrD N-terminal leader domain in S. aureus cell-free culture supernatants. Functional assessment of these peptides revealed unexpected bioactivities, including human cell-line cytotoxicity, modulation  ...[more]

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