scholarly journals Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides

2021 ◽  
Author(s):  
Bengt H. Gless ◽  
Benjamin S. Bejder ◽  
Fabrizio Monda ◽  
Martin S. Bojer ◽  
Hanne Ingmer ◽  
...  
Keyword(s):  
Autoinducing Peptides

Lactam hybrid analogues of solonamide B and autoinducing peptides as potent S. aureus AgrC antagonists

2018 ◽  
Vol 152 ◽  
pp. 370-376 ◽  
Author(s):  
Anna Mette Hansen ◽  
Pai Peng ◽  
Mara Baldry ◽  
Iris Perez-Gassol ◽  
Simon B. Christensen ◽  
...  
Keyword(s):  
Autoinducing Peptides

scholarly journals Characterization of structural elements in native autoinducing peptides and non-native analogues that permit the differential modulation of AgrC-type quorum sensing receptors in Staphylococcus aureus

2016 ◽  
Vol 14 (1) ◽  
pp. 113-121 ◽  
Author(s):  
Yftah Tal-Gan ◽  
Monika Ivancic ◽  
Gabriel Cornilescu ◽  
Helen E. Blackwell
Keyword(s):  
Staphylococcus Aureus ◽  
Quorum Sensing ◽  
Structural Elements ◽  
Differential Modulation ◽  
Autoinducing Peptides

Structural analyses of autoinducing peptides and analogues thereof reveal motifs critical for modulation of quorum sensing receptors inS. aureus.

scholarly journals Rearrangement of Thiodepsipeptides by S–N Acyl Shift Delivers Homodetic Autoinducing Peptides

2021 ◽  
Author(s):  
Bengt H. Gless ◽  
Benjamin Svejdal Bejder ◽  
Martin S. Bojer ◽  
Hanne Ingmer ◽  
Christian Adam Olsen
Keyword(s):  
Listeria Monocytogenes ◽  
Quorum Sensing ◽  
Clostridium Perfringens ◽  
Biofilm Formation ◽  
Group Behavior ◽  
Peptide Ligands ◽  
Gram Positive Bacteria ◽  
Chemically Induced ◽  
Modified Peptides ◽  
Autoinducing Peptides

Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has been predicted to constitute a structural feature of AIPs from other species as well. Here, we show that pentameric AIPs from <i>Lactobacillus plantarum, Clostridium perfringens, </i>and<i> Listeria monocytogenes </i>that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of the cross-species communication of bacteria and may help guide the discovery of peptide ligands to perturb their function.

scholarly journals Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence

2015 ◽  
Vol 112 (34) ◽  
pp. 10679-10684 ◽  
Author(s):  
Boyuan Wang ◽  
Aishan Zhao ◽  
Richard P. Novick ◽  
Tom W. Muir
Keyword(s):  
Quorum Sensing ◽  
Driving Forces ◽  
Side Chain ◽  
Accessory Gene ◽  
Accessory Gene Regulator ◽  
C Terminus ◽  
In Vitro Reconstitution ◽  
Intimate Link ◽  
Autoinducing Peptides

Staphylococci produce autoinducing peptides (AIPs) as quorum-sensing signals that regulate virulence. These AIPs feature a thiolactone macrocycle that connects the peptide C terminus to the side chain of an internal cysteine. AIPs are processed from ribosomally synthesized precursors [accessory gene regulator D (AgrD)] through two proteolytic events. Formation of the thiolactone is coupled to the first of these and involves the activity of the integral membrane protease AgrB. This step is expected to be thermodynamically unfavorable, and therefore, it is unclear how AIP-producing bacteria produce sufficient amounts of the thiolactone-containing intermediate to drive quorum sensing. Herein, we present the in vitro reconstitution of the AgrB-dependent proteolysis of an AgrD precursor from Staphylococcus aureus. Our data show that efficient thiolactone production is driven by two unanticipated features of the system: (i) membrane association of the thiolactone-containing intermediate, which stabilizes the macrocycle, and (ii) rapid degradation of the C-terminal proteolysis fragment AgrDC, which affects the reaction equilibrium position. Cell-based studies confirm the intimate link between AIP production and intracellular AgrDC levels. Thus, our studies explain the chemical principles that drive AIP production, including uncovering a hitherto unknown link between quorum sensing and peptide turnover.

scholarly journals Rearrangement of Thiodepsipeptides by S–N Acyl Shift Delivers Homodetic Autoinducing Peptides

2021 ◽  
Author(s):  
Christian Adam Olsen ◽  
Bengt H. Gless ◽  
Benjamin Svejdal Bejder ◽  
Fabrizio Monda ◽  
Martin S. Bojer ◽  
...  
Keyword(s):  
Autoinducing Peptides

scholarly journals Biosynthesis of Staphylococcus aureus Autoinducing Peptides by Using the Synechocystis DnaB Mini-Intein

2007 ◽  
Vol 73 (19) ◽  
pp. 6036-6044 ◽  
Author(s):  
Cheryl L. Malone ◽  
Blaise R. Boles ◽  
Alexander R. Horswill
Keyword(s):  
Staphylococcus Aureus ◽  
Fusion Protein ◽  
Biochemical Analysis ◽  
Side Chain ◽  
Biological Applications ◽  
Dna Encoding ◽  
Sensing System ◽  
Quorum Sensing System ◽  
Reporter Strains ◽  
Autoinducing Peptides

ABSTRACT The Agr quorum-sensing system of Staphylococcus aureus modulates the expression of virulence factors in response to autoinducing peptides (AIPs). The peptides are seven to nine residues in length and have the C-terminal five residues constrained in a thiolactone ring. We have developed a new method to generate AIP structures using an engineered DnaB mini-intein from Synechocystis sp. strain PCC6803. In the method, an oligonucleotide encoding the AIP is ligated to the intein and the fusion protein is expressed and purified by affinity chromatography. To produce the correct AIP structure, intein splicing is interrupted, allowing the cysteine side chain to catalyze thiolactone ring formation and release AIP from the resin. The technique is simple and robust, and we have successfully produced the three main classes of AIPs using the intein system. The intein-generated AIPs possessed the correct thiolactone ring modification based on biochemical analysis, and, importantly, all the samples were bioactive against S. aureus. The AIP activity was confirmed through Agr interference and activation profiling with developed S. aureus reporter strains. The simplicity of the method, benefits of DNA encoding, and scalable nature enable the production of S. aureus AIPs for many biological applications.

scholarly journals Quorum sensing between bacterial species on the skin protects against epidermal injury in atopic dermatitis

2019 ◽  
Vol 11 (490) ◽  
pp. eaat8329 ◽  
Author(s):  
Michael R. Williams ◽  
Stephen K. Costa ◽  
Livia S. Zaramela ◽  
Shadi Khalil ◽  
Daniel A. Todd ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Quorum Sensing ◽  
Normal Skin ◽  
Bacterial Species ◽  
Skin Barrier ◽  
Toxin Production ◽  
Skin Microbiome ◽  
Coagulase Negative Staphylococci ◽  
Normal Human Skin ◽  
Autoinducing Peptides

Colonization of the skin by Staphylococcus aureus is associated with exacerbation of atopic dermatitis (AD), but any direct mechanism through which dysbiosis of the skin microbiome may influence the development of AD is unknown. Here, we show that proteases and phenol-soluble modulin α (PSMα) secreted by S. aureus lead to endogenous epidermal proteolysis and skin barrier damage that promoted inflammation in mice. We further show that clinical isolates of different coagulase-negative staphylococci (CoNS) species residing on normal skin produced autoinducing peptides that inhibited the S. aureus agr system, in turn decreasing PSMα expression. These autoinducing peptides from skin microbiome CoNS species potently suppressed PSMα expression in S. aureus isolates from subjects with AD without inhibiting S. aureus growth. Metagenomic analysis of the AD skin microbiome revealed that the increase in the relative abundance of S. aureus in patients with active AD correlated with a lower CoNS autoinducing peptides to S. aureus ratio, thus overcoming the peptides’ capacity to inhibit the S. aureus agr system. Characterization of a S. hominis clinical isolate identified an autoinducing peptide (SYNVCGGYF) as a highly potent inhibitor of S. aureus agr activity, capable of preventing S. aureus–mediated epithelial damage and inflammation on murine skin. Together, these findings show how members of the normal human skin microbiome can contribute to epithelial barrier homeostasis by using quorum sensing to inhibit S. aureus toxin production.

scholarly journals Rearrangement of Thiodepsipeptides by S–N Acyl Shift Delivers Homodetic Autoinducing Peptides

2021 ◽  
Author(s):  
Bengt H. Gless ◽  
Benjamin Svejdal Bejder ◽  
Martin S. Bojer ◽  
Hanne Ingmer ◽  
Christian Adam Olsen
Keyword(s):  
Listeria Monocytogenes ◽  
Quorum Sensing ◽  
Clostridium Perfringens ◽  
Biofilm Formation ◽  
Group Behavior ◽  
Peptide Ligands ◽  
Gram Positive Bacteria ◽  
Chemically Induced ◽  
Modified Peptides ◽  
Autoinducing Peptides

Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has been predicted to constitute a structural feature of AIPs from other species as well. Here, we show that pentameric AIPs from <i>Lactobacillus plantarum, Clostridium perfringens, </i>and<i> Listeria monocytogenes </i>that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of the cross-species communication of bacteria and may help guide the discovery of peptide ligands to perturb their function.

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