Plener L

References (6)

Title : Organophosphorus poisoning in animals and enzymatic antidotes - Poirier_2021_Environ.Sci.Pollut.Res.Int_28_25081
Author(s) : Poirier L , Jacquet P , Plener L , Masson P , Daude D , Chabriere E
Ref : Environ Sci Pollut Res Int , 28 :25081 , 2021
Abstract : Organophosphorus compounds (OPs) are neurotoxic molecules developed as pesticides and chemical warfare nerve agents (CWNAs). Most of them are covalent inhibitors of acetylcholinesterase (AChE), a key enzyme in nervous systems, and are therefore responsible for numerous poisonings around the world. Many animal models have been studied over the years in order to decipher the toxicity of OPs and to provide insights for therapeutic and decontamination purposes. Environmental impact on wild animal species has been analyzed to understand the consequences of OP uses in agriculture. In complement, various laboratory models, from invertebrates to aquatic organisms, rodents and primates, have been chosen to study chronic and acute toxicity as well as neurobehavioral impact, immune response, developmental disruption, and other pathological signs. Several decontamination approaches were developed to counteract the poisoning effects of OPs. Among these, enzyme-based strategies are particularly attractive as they allow efficient external decontamination without toxicity or environmental impact and may be of interest for treatment. Approaches using bioscavengers for prophylaxis, treatment, and external decontamination are emphasized and their potential is discussed in the light of toxicological observations from various animal models. The relevance of animal models, regarding their cholinergic system and the abundance of naturally protecting enzymes, is also discussed for better extrapolation of results to human.
ESTHER : Poirier_2021_Environ.Sci.Pollut.Res.Int_28_25081
PubMedSearch : Poirier_2021_Environ.Sci.Pollut.Res.Int_28_25081
PubMedID: 29959732

Title : Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control - Billot_2020_J.Biol.Chem_295_12993
Author(s) : Billot R , Plener L , Jacquet P , Elias M , Chabriere E , Daude D
Ref : Journal of Biological Chemistry , 295 :12993 , 2020
Abstract : Enzymes able to degrade or modify acyl-homoserine lactones (AHLs) have drawn considerable interest for their ability to interfere with the bacterial communication process referred to as quorum sensing. Many proteobacteria use AHL to coordinate virulence and biofilm formation in a cell density-dependent manner; thus, AHL-interfering enzymes constitute new promising antimicrobial candidates. Among these, lactonases and acylases have been particularly studied. These enzymes have been isolated from various bacterial, archaeal, or eukaryotic organisms and have been evaluated for their ability to control several pathogens. Engineering studies on these enzymes were carried out and successfully modulated their capacity to interact with specific AHL, increase their catalytic activity and stability, or enhance their biotechnological potential. In this review, special attention is paid to the screening, engineering, and applications of AHL-modifying enzymes. Prospects and future opportunities are also discussed with a view to developing potent candidates for bacterial control.
ESTHER : Billot_2020_J.Biol.Chem_295_12993
PubMedSearch : Billot_2020_J.Biol.Chem_295_12993
PubMedID: 32690609

Title : Enzymatic decontamination of paraoxon-ethyl limits long-term effects in planarians - Poirier_2020_Sci.Rep_10_3843
Author(s) : Poirier L , Plener L , Daude D , Chabriere E
Ref : Sci Rep , 10 :3843 , 2020
Abstract : Organophosphorus compounds (OP) are highly toxic molecules used as insecticides that inhibit cholinesterase enzymes involved in neuronal transmission. The intensive use of OP for vector control and agriculture has led to environmental pollutions responsible for severe intoxications and putative long-term effects on humans and wild animals. Many in vivo models were studied over the years to assess OP acute toxicity, but the long-term effects are poorly documented. Planarian, a freshwater flatworm having a cholinergic system, has emerged as a new original model for addressing both toxicity and developmental perturbations. We used Schmidtea mediterranea planarians to evaluate long-term effects of paraoxon-ethyl at two sublethal concentrations over three generations. Toxicity, developmental perturbations and disruption of behavior were rapidly observed and higher sensitivity to paraoxon-ethyl of next generations was noticed suggesting that low insecticide doses can induce transgenerational effects. With the view of limiting OP poisoning, SsoPox, an hyperthermostable enzyme issued from the archaea Saccharolobus solfataricus, was used to degrade paraoxon-ethyl prior to planarian exposure. The degradation products, although not lethal to the worms, were found to decrease cholinesterase activities for the last generation of planarians and to induce abnormalities albeit in lower proportion than insecticides.
ESTHER : Poirier_2020_Sci.Rep_10_3843
PubMedSearch : Poirier_2020_Sci.Rep_10_3843
PubMedID: 32123261

Title : Biotechnological applications of quorum quenching enzymes - Bzdrenga_2017_Chem.Biol.Interact_267_104
Author(s) : Bzdrenga J , Daude D , Remy B , Jacquet P , Plener L , Elias M , Chabriere E
Ref : Chemico-Biological Interactions , 267 :104 , 2017
Abstract : Numerous bacteria use quorum sensing (QS) to synchronize their behavior and monitor their population density. They use signaling molecules known as autoinducers (AI's) that are synthesized and secreted into their local environment to regulate QS-dependent gene expression. Among QS-regulated pathways, biofilm formation and virulence factor secretion are particularly problematic as they are involved in surface-attachment, antimicrobial agent resistance, toxicity, and pathogenicity. Targeting QS represents a promising strategy to inhibit undesirable bacterial traits. This strategy, referred to as quorum quenching (QQ), includes QS-inhibitors and QQ enzymes. These approaches are appealing because they do not directly challenge bacterial survival, and consequently selection pressure may be low, yielding a lower occurrence of resistance. QQ enzymes are particularly promising because they act extracellularly to degrade AI's and can be used in catalytic quantities. This review draws an overview of QQ enzyme related applications, covering several economically important fields such as agriculture, aquaculture, biofouling and health issues. Finally, the possibility of resistance mechanism occurrence to QQ strategies is discussed.
ESTHER : Bzdrenga_2017_Chem.Biol.Interact_267_104
PubMedSearch : Bzdrenga_2017_Chem.Biol.Interact_267_104
PubMedID: 27223408

Title : Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications - Remy_2016_Sci.Rep_6_37780
Author(s) : Remy B , Plener L , Poirier L , Elias M , Daude D , Chabriere E
Ref : Sci Rep , 6 :37780 , 2016
Abstract : Extremozymes have gained considerable interest as they could meet industrial requirements. Among these, SsoPox is a hyperthermostable enzyme isolated from the archaeon Sulfolobus solfataricus. This enzyme is a lactonase catalyzing the hydrolysis of acyl-homoserine lactones; these molecules are involved in Gram-negative bacterial communication referred to as quorum sensing. SsoPox exhibits promiscuous phosphotriesterase activity for the degradation of organophosphorous chemicals including insecticides and chemical warfare agents. Owing to its bi-functional catalytic abilities as well as its intrinsic stability, SsoPox is appealing for many applications, having potential uses in the agriculture, defense, food and health industries. Here we investigate the biotechnological properties of the mutant SsoPox-W263I, a variant with increased lactonase and phosphotriesterase activities. We tested enzyme resistance against diverse process-like and operating conditions such as heat resistance, contact with organic solvents, sterilization, storage and immobilization. Bacterial secreted materials from both Gram-negative and positive bacteria were harmless on SsoPox-W263I activity and could reactivate heat-inactivated enzyme. SsoPox showed resistance to harsh conditions demonstrating that it is an extremely attractive enzyme for many applications. Finally, the potential of SsoPox-W263I to be active at subzero temperature is highlighted and discussed in regards to the common idea that hyperthermophile enzymes are nearly inactive at low temperatures.
ESTHER : Remy_2016_Sci.Rep_6_37780
PubMedSearch : Remy_2016_Sci.Rep_6_37780
PubMedID: 27876889

Title : The Janthinobacterium sp. HH01 genome encodes a homologue of the V. cholerae CqsA and L. pneumophila LqsA autoinducer synthases - Hornung_2013_PLoS.One_8_e55045
Author(s) : Hornung C , Poehlein A , Haack FS , Schmidt M , Dierking K , Pohlen A , Schulenburg H , Blokesch M , Plener L , Jung K , Bonge A , Krohn-Molt I , Utpatel C , Timmermann G , Spieck E , Pommerening-Roser A , Bode E , Bode HB , Daniel R , Schmeisser C , Streit WR
Ref : PLoS ONE , 8 :e55045 , 2013
Abstract : Janthinobacteria commonly form biofilms on eukaryotic hosts and are known to synthesize antibacterial and antifungal compounds. Janthinobacterium sp. HH01 was recently isolated from an aquatic environment and its genome sequence was established. The genome consists of a single chromosome and reveals a size of 7.10 Mb, being the largest janthinobacterial genome so far known. Approximately 80% of the 5,980 coding sequences (CDSs) present in the HH01 genome could be assigned putative functions. The genome encodes a wealth of secretory functions and several large clusters for polyketide biosynthesis. HH01 also encodes a remarkable number of proteins involved in resistance to drugs or heavy metals. Interestingly, the genome of HH01 apparently lacks the N-acylhomoserine lactone (AHL)-dependent signaling system and the AI-2-dependent quorum sensing regulatory circuit. Instead it encodes a homologue of the Legionella- and Vibrio-like autoinducer (lqsA/cqsA) synthase gene which we designated jqsA. The jqsA gene is linked to a cognate sensor kinase (jqsS) which is flanked by the response regulator jqsR. Here we show that a jqsA deletion has strong impact on the violacein biosynthesis in Janthinobacterium sp. HH01 and that a jqsA deletion mutant can be functionally complemented with the V. cholerae cqsA and the L. pneumophila lqsA genes.
ESTHER : Hornung_2013_PLoS.One_8_e55045
PubMedSearch : Hornung_2013_PLoS.One_8_e55045
PubMedID: 23405110
Gene_locus related to this paper: 9burk-l9pl81 , 9burk-l9pql3 , 9burk-l9pc92 , 9burk-l9pf07 , 9burk-l9pgi7 , 9burk-l9p8t0 , 9burk-l9pl28