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Academic literature on the topic 'Luciferasi'

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Published: 11 March 2023

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Journal articles on the topic "Luciferasi"

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Heise, Kerstin, Henry Oppermann, Jürgen Meixensberger, Rolf Gebhardt, and Frank Gaunitz. "Dual Luciferase Assay for Secreted Luciferases Based onGaussiaand NanoLuc." ASSAY and Drug Development Technologies 11, no. 4 (May 2013): 244–52. http://dx.doi.org/10.1089/adt.2013.509.

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Delroisse, Jérôme, Esther Ullrich-Lüter, Stefanie Blaue, Olga Ortega-Martinez, Igor Eeckhaut, Patrick Flammang, and Jérôme Mallefet. "A puzzling homology: a brittle star using a putative cnidarian-type luciferase for bioluminescence." Open Biology 7, no. 4 (April 2017): 160300. http://dx.doi.org/10.1098/rsob.160300.

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Bioluminescence relies on the oxidation of a luciferin substrate catalysed by a luciferase enzyme. Luciferins and luciferases are generic terms used to describe a large variety of substrates and enzymes. Whereas luciferins can be shared by phylogenetically distant organisms which feed on organisms producing them, luciferases have been thought to be lineage-specific enzymes. Numerous light emission systems would then have co-emerged independently along the tree of life resulting in a plethora of non-homologous luciferases. Here, we identify for the first time a candidate luciferase of a luminous echinoderm, the ophiuroid Amphiura filiformis . Phylogenomic analyses identified the brittle star predicted luciferase as homologous to the luciferase of the sea pansy Renilla (Cnidaria), contradicting with the traditional viewpoint according to which luciferases would generally be of convergent origins. The similarity between the Renilla and Amphiura luciferases allowed us to detect the latter using anti- Renilla luciferase antibodies. Luciferase expression was specifically localized in the spines which were demonstrated to be the bioluminescent organs in vivo . However, enzymes homologous to the Renilla luciferase but unable to trigger light emission were also identified in non-luminous echinoderms and metazoans. Our findings strongly indicate that those enzymes, belonging to the haloalkane dehalogenase family, might then have been convergently co-opted into luciferases in cnidarians and echinoderms. In these two benthic suspension-feeding species, similar ecological pressures would constitute strong selective forces for the functional shift of these enzymes and the emergence of bioluminescence.
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HOSSEINKHANI, Saman, Rose SZITTNER, and Edward A. MEIGHEN. "Random mutagenesis of bacterial luciferase: critical role of Glu175 in the control of luminescence decay." Biochemical Journal 385, no. 2 (January 7, 2005): 575–80. http://dx.doi.org/10.1042/bj20040863.

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Bacterial luciferases (LuxAB) can be readily classed as slow or fast decay luciferases based on their rates of luminescence decay in a single turnover assay. Luciferases from Vibrio harveyi and Xenorhabdus (Photorhabdus) luminescens have slow decay rates, and those from the Photobacterium genus, such as Photobacterium fisheri, P. phosphoreum and P. leiognathi, have rapid decay rates. By substitution of a 67-amino-acid stretch of P. phosphoreum LuxA in the central region of the LuxA subunit, the ‘slow’ X. luminescens luciferase was converted into a chimaeric luciferase with a significantly more rapid decay rate [Valkova, Szittner and Meighen (1999) Biochemistry 38, 13820–13828]. To understand better the role of specific residues in the classification of luciferases as slow and fast decay, we have conducted random mutagenesis on this region. One of the mutants generated by a single mutation on LuxA at position 175 [E175G (Glu175→Gly)] resulted in the ‘slow decay’ X. luminescens luciferase being converted into a luciferase with a significantly more rapid decay rate. These results indicate the importance of Glu175 in LuxA as a critical residue for differentiating between ‘slow’ and ‘fast’ luciferases and show that this distinction is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase–flavin–oxygen intermediate.
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Viviani, Vadim R., Gabriel F. Pelentir, and Vanessa R. Bevilaqua. "Bioluminescence Color-Tuning Firefly Luciferases: Engineering and Prospects for Real-Time Intracellular pH Imaging and Heavy Metal Biosensing." Biosensors 12, no. 6 (June 10, 2022): 400. http://dx.doi.org/10.3390/bios12060400.

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Firefly luciferases catalyze the efficient production of yellow-green light under normal physiological conditions, having been extensively used for bioanalytical purposes for over 5 decades. Under acidic conditions, high temperatures and the presence of heavy metals, they produce red light, a property that is called pH-sensitivity or pH-dependency. Despite the demand for physiological intracellular biosensors for pH and heavy metals, firefly luciferase pH and metal sensitivities were considered drawbacks in analytical assays. We first demonstrated that firefly luciferases and their pH and metal sensitivities can be harnessed to estimate intracellular pH variations and toxic metal concentrations through ratiometric analysis. Using Macrolampis sp2 firefly luciferase, the intracellular pH could be ratiometrically estimated in bacteria and then in mammalian cells. The luciferases of Macrolampis sp2 and Cratomorphus distinctus fireflies were also harnessed to ratiometrically estimate zinc, mercury and other toxic metal concentrations in the micromolar range. The temperature was also ratiometrically estimated using firefly luciferases. The identification and engineering of metal-binding sites have allowed the development of novel luciferases that are more specific to certain metals. The luciferase of the Amydetes viviani firefly was selected for its special sensitivity to cadmium and mercury, and for its stability at higher temperatures. These color-tuning luciferases can potentially be used with smartphones for hands-on field analysis of water contamination and biochemistry teaching assays. Thus, firefly luciferases are novel color-tuning sensors for intracellular pH and toxic metals. Furthermore, a single luciferase gene is potentially useful as a dual bioluminescent reporter to simultaneously report intracellular ATP and/or luciferase concentrations luminometrically, and pH or metal concentrations ratiometrically, providing a useful tool for real-time imaging of intracellular dynamics and stress.
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Tafreshi, Narges Kh, Majid Sadeghizadeh, Rahman Emamzadeh, Bijan Ranjbar, Hossein Naderi-Manesh, and Saman Hosseinkhani. "Site-directed mutagenesis of firefly luciferase: implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases." Biochemical Journal 412, no. 1 (April 25, 2008): 27–33. http://dx.doi.org/10.1042/bj20070733.

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The bioluminescence colours of firefly luciferases are determined by assay conditions and luciferase structure. Owing to red light having lower energy than green light and being less absorbed by biological tissues, red-emitting luciferases have been considered as useful reporters in imaging technology. A set of red-emitting mutants of Lampyris turkestanicus (Iranian firefly) luciferase has been made by site-directed mutagenesis. Among different beetle luciferases, those from Phrixothrix (railroad worm) emit either green or red bioluminescence colours naturally. By substitution of three specific amino acids using site-specific mutagenesis in a green-emitting luciferase (from L. turkestanicus), the colour of emitted light was changed to red concomitant with decreasing decay rate. Different specific mutations (H245N, S284T and H431Y) led to changes in the bioluminescence colour. Meanwhile, the luciferase reaction took place with relative retention of its basic kinetic properties such as Km and relative activity. Structural comparison of the native and mutant luciferases using intrinsic fluorescence, far-UV CD spectra and homology modelling revealed a significant conformational change in mutant forms. A change in the colour of emitted light indicates the critical role of these conserved residues in bioluminescence colour determination among firefly luciferases. Relatively high specific activity and emission of red light might make these mutants suitable as reporters for the study of gene expression and bioluminescence imaging.
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Kim, Sung Bae, Ryo Nishihara, Daniel Citterio, and Koji Suzuki. "Fabrication of a New Lineage of Artificial Luciferases from Natural Luciferase Pools." ACS Combinatorial Science 19, no. 9 (August 9, 2017): 594–99. http://dx.doi.org/10.1021/acscombsci.7b00081.

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Kotlobay, A. A., Z. M. Kaskova, and I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine." Acta Naturae 12, no. 2 (August 7, 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.10967.

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Optoanalytical methods based on using genetically encoded bioluminescent enzymes,luciferases, allow one to obtain highly sensitive signals, are non-invasive, and require no external irradiation. Bioluminescence is based on the chemical reaction of oxidation of a low-molecular-weight substrate (luciferin) by atmospheric oxygen, which is catalyzed by an enzyme (luciferase). Relaxation of the luciferin oxidation product from its excited state is accompanied by a release of a quantum of light, which can be detected as an analytical signal.The ability to express luciferase genes in various heterological systems and high quantum yields of luminescence reactions have made these tools rather popular in biology and medicine. Amongseveral naturally available luciferases, a few have been found to be useful for practicalapplication. Luciferase size, the wavelength of its luminescence maximum, enzyme thermostability, optimal pH of the reaction, and the need for cofactors areparameters that may differ for luciferases from different groups of organisms, and this fact directly affects the choice of the application area for each enzyme. It is quite important to overview the whole range of currently available luciferases based ontheir biochemical properties before choosing one bioluminescent probe suitable for a specific application.
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Kotlobay, A. A., Z. M. Kaskova, and I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine." Acta Naturae 12, no. 2 (August 7, 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.11152.

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Optoanalytical methods based on using genetically encoded bioluminescent enzymes,luciferases, allow one to obtain highly sensitive signals, are non-invasive, and require no external irradiation. Bioluminescence is based on the chemical reaction of oxidation of a low-molecular-weight substrate (luciferin) by atmospheric oxygen, which is catalyzed by an enzyme (luciferase). Relaxation of the luciferin oxidation product from its excited state is accompanied by a release of a quantum of light, which can be detected as an analytical signal.The ability to express luciferase genes in various heterological systems and high quantum yields of luminescence reactions have made these tools rather popular in biology and medicine. Amongseveral naturally available luciferases, a few have been found to be useful for practicalapplication. Luciferase size, the wavelength of its luminescence maximum, enzyme thermostability, optimal pH of the reaction, and the need for cofactors areparameters that may differ for luciferases from different groups of organisms, and this fact directly affects the choice of the application area for each enzyme. It is quite important to overview the whole range of currently available luciferases based ontheir biochemical properties before choosing one bioluminescent probe suitable for a specific application.
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SALA-NEWBY, Graciela B., Catherine M. THOMSON, and Anthony K. CAMPBELL. "Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis." Biochemical Journal 313, no. 3 (February 1, 1996): 761–67. http://dx.doi.org/10.1042/bj3130761.

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A full-length clone encoding Lampyris noctiluca (British glow-worm) luciferase was isolated from a complementary DNA (cDNA) expression library constructed with mRNA extracted from light organs. The luciferase was a 547-residue protein, as deduced from the nucleotide sequence. The protein was closely related to those of other lampyrid beetles, the similarity to Photinus pyralis luciferase being 84% and to Luciola 67%. In contrast, Lampyris luciferase had less sequence similarity to the luciferases of the click beetle Pyrophorus, at 48%. Engineering Lampyris luciferase in vitro showed that the C-terminal peptide containing 12 amino acids in Photinus and 9 amino acids in Lampyris was essential for bioluminescence. The pH optimum and the Km values for ATP and luciferin were similar for both Photinus and Lampyris luciferases, although the light emitted by the latter shifted towards the blue and was less stable at 37 °C. It was concluded that the molecular and biochemical properties were not sufficient to explain the glowing or flashing of the two beetles Lampyris and Photinus.
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Carrasco-López, César, Juliana C. Ferreira, Nathan M. Lui, Stefan Schramm, Romain Berraud-Pache, Isabelle Navizet, Santosh Panjikar, Panče Naumov, and Wael M. Rabeh. "Beetle luciferases with naturally red- and blue-shifted emission." Life Science Alliance 1, no. 4 (August 2018): e201800072. http://dx.doi.org/10.26508/lsa.201800072.

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The different colors of light emitted by bioluminescent beetles that use an identical substrate and chemiexcitation reaction sequence to generate light remain a challenging and controversial mechanistic conundrum. The crystal structures of two beetle luciferases with red- and blue-shifted light relative to the green yellow light of the common firefly species provide direct insight into the molecular origin of the bioluminescence color. The structure of a blue-shifted green-emitting luciferase from the firefly Amydetes vivianii is monomeric with a structural fold similar to the previously reported firefly luciferases. The only known naturally red-emitting luciferase from the glow-worm Phrixothrix hirtus exists as tetramers and octamers. Structural and computational analyses reveal varying aperture between the two domains enclosing the active site. Mutagenesis analysis identified two conserved loops that contribute to the color of the emitted light. These results are expected to advance comparative computational studies into the conformational landscape of the luciferase reaction sequence.
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Dissertations / Theses on the topic "Luciferasi"

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Conti, Elena Eliana. "Crystal structure of firefly luciferase." Thesis, Imperial College London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244284.

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Walpole, C. S. J. "Active site probes for bacterial luciferase." Thesis, University of Sussex, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356510.

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Lin, Leo Yen-Cheng. "Flavin binding site in Vibrio harveyi Luciferase." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=85083.

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Luciferase catalyzes the emission of blue-green light and is the central feature of bacterial bioluminescence. The three-dimensional structure of the bacterial luciferase apo-enzyme determined by X-ray crystallography has revealed the detailed landscape of the enzyme active site, however, the absence of a structure with bound substrate has impeded the understanding of the enzyme mechanism by which luciferase interacts with substrates and catalyzes their conversion into light emission. This thesis describes three research projects that focus on the molecular conformation of flavin in the active site of bacterial luciferase. Based on available structure-activity data as guidance, the first project deduces the binding conformation of the luciferase bound flavin by computer modeling. The second research project investigates the binding microenvironment of flavin, and assigns specific functions to the structural modules (amino acid residues), which coordinate flavin in the proposed model. The third project verifies the validity of the proposed model with mutational analysis of the binding site residues, and points out the possibility of altering the visible emission color of bacterial bioluminescence by redesigning luciferase. The last chapter concludes the thesis with the discussion of the structural mechanism of luciferase catalysis, and the perspectives for the engineering of luciferase variants that emit different light colors.
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Chan, Wai Shing. "Applications of the bacterial luciferin-luciferase system." HKBU Institutional Repository, 2012. https://repository.hkbu.edu.hk/etd_ra/1454.

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Gupta, Rajat. "Firefly luciferase mutants as sensors of proteome stress." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-150266.

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Lasko, Daniel R. "On-line fermentation monitoring via recombinant firefly luciferase." Thesis, Massachusetts Institute of Technology, 1995. http://hdl.handle.net/1721.1/11125.

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Andrews, Thomas. "A novel dual-luciferase monitoring apparatus a thesis /." San Antonio : UTHSC, 2008. http://learningobjects.library.uthscsa.edu/cdm4/item_viewer.php?CISOROOT=/theses&CISOPTR=36&CISOBOX=1&REC=20.

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Oliveira, Anderson Garbuglio de. "Estudo mecanístico da bioluminescência de fungos." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/46/46135/tde-08112010-093327/.

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Esta tese descreve como é possível obter emissão de luz in vitro enzimaticamente, a partir de extratos quente e frio de diferentes espécies de fungos bioluminescentes, o que indica também um mecanismo comum de bioluminescência em todos esses organismos. Dados cinéticos sugerem um mecanismo enzimático em duas etapas e corroboram a hipótese enzimática de Airth e Foerster, da década de 1960. Finalmente, utilizando-se extratos quente e frio foi possível também isolar a luciferina fúngica e obter sua massa molecular (298,1837 m/z). Essa substância isolada emite luz enzimaticamente in vitro, sendo que a sobreposição do espectro de emissão e do espectro de bioluminescência do fungo confirma que essa substância é a luciferina fúngica.
This thesis describes how in vitro light emission can be enzymatically obtained from the hot and cold extracts assay using different species of fungi, which also indicates a common mechanism of light emission for all these organisms. Kinetic data suggest a consecutive two-step mechanism and corroborate the 1960\'s enzymatic proposal of Airth and Foerster. Finally, using hot and cold extracts assay we were also able to purify and to determine the molecular weight of the fungal luciferin (298.1837 m/z). The isolated substance emits light enzymatically in vitro, whose light emission spectrum matches with the fungal bioluminescence one thus confirming that the substance is the fungal luciferin
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Buriánková, Karolína. "Résistance ribosomique aux macrolides et leur effet sur la fidélité de traduction." Paris 11, 2003. http://www.theses.fr/2003PA112220.

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Les macrolides forment un groupe homogène d'agents antibactériens produits par des Streptomyces et d'autres actinomycètes. Ils inhibent la synthèse protéique des bactéries par liaison à la sous-unité ribosomique 50S, ce qui empêche son assemblage ou son fonctionnement. La première partie de ce manuscrit porte sur l'effet des macrolides sur la fidélité de traduction. Nous avons utilisé comme système rapporteur la luciférase de Vibrio harveyi avec un codon stop introduit au début du gène luxB pour mesurer in vivo la suppression de ce codon stop. L'érythromycine augmente la trans-lecture du codon stop UAG et diminue donc la fidélité de traduction, en accord avec l'hypothèse selon laquelle les macrolides agissent en début d'élongation. Cet effet a été confirmé par l'étude du taux global d'erreur en utilisant l'électrophorèse 2-D des protéines. La deuxième partie porte sur la résistance naturelle aux macrolides chez les mycobactéries du complexe M. Tuberculosis (CMT), résistance généralement attribuée à la structure spécifique de la paroi des mycobactéries. Nous avons identifié un gène codant une méthyltransférase de type Erm, modifiant les ribosomes et conférant la résistance aux macrolides. Ce gène, appelé ermMT, est conservé chez tous les membres du CMT mais est affecté par une délétion dans certaines souches vaccinales de M. Bovis BCG comme BCG Pasteur. Cette dernière souche est sensible aux macrolides, alors que les autres membres du CMT sont résistants. L'expression de ermMT dans des mycobactéries sensibles aux macrolides confère la résistance. La comparaison des niveaux de résistance et de l'affinité pour l'érythromycine des ribosomes de souches exprimant ermMT ou d'autres gènes erm indique que ermMT confère une résistance de type I aux macrolides, lincosamides et streptogramines, correspondant à la mono-méthylation de A2058 dans l'ARN 23S. Nos résultats montrent que ermMT joue un rôle majeur dans la résistance naturelle aux macrolides chez les mycobactéries du CMT
Macrolide antibiotics constitute a homogenous group of antibacterial agents produced by Streptomyces or related Actinobacteria. They inhibit protein synthesis in bacteria by binding to the 50S ribosomal subunit, preventing its assembly or inhibiting its function. In the first part of this thesis the effect of macrolides on translation accuracy was studied. We have used the reporter system based on Vibrio harveyi luciferase with a stop codon inserted in the proximal part of the luxB gene for the in vivo measurement of the nonsense codon readthrough. Erythromycin stimulated the leadthrough of the UAG stop codon and thus the decrease of the translation accuracy. This is in agreement with the hypothesis that macrolides influence the early stages of elongation process. The misreading effect of macrolides was confirmed by the study of global error frequencies using the 2-D gel electrophoresis of proteins. The second part deals with the intrinsic macrolide resistance of the Mycobacterium tuberculosis complex (MTC), generally attributed to the low permeability of the mycobacterial cell wall. However we have shown that a gene, whose product confers macrolide resistance by ribosome modification, was present in all members of the MTC. It was named ermMT (erm. 37). Part of the ermMT is deleted in some vaccinal strains of Mycobacterium bovis BCG, such as the Pasteur strain. The Pasteur strain was susceptible to macrolides, whereas MTC species were resistant to them. The expression of ermMT in the macrolide-sensitive Mycobacterium strains conferred macrolide resistance. Comparison of the resistance patterns and ribosomal affinity for erythromycin of Mycobacterium host strains expressing ermMT or other erm genes indicates that ermMT confers a type I resistance to macrolides, lincosamides and streptogramins, coiresponding to the mono-methylation of A2058 in 23S rRNA. Our results indicate that ermMT plays a major role in the intrinsic macrolide resistance of members of the MTC
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Eriksson, Jonas. "Advancements in Firefly Luciferase-Based Assays and Pyrosequencing Technology." Doctoral thesis, KTH, Biotechnology, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3708.

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Pyrosequencing is a new DNA sequencing method relying on thesequencing-by-synthesis principle and bioluminometric detectionof nucleotide incorporation events. The objective of thisthesis was improvement of the Pyrosequencing method byincreasing the thermal stability of firefly luciferase, and byintroducing an alternative DNA polymerase and a new nucleotideanalog. Furthermore, the development of a new bioluminescentassay is described for the detection of inorganicpyrophosphatase activity.

The wild-type North American firefly(Photinus pyralis)luciferase is a heat-sensitiveenzyme, the catalytic activity of which is rapidly lost attemperatures over 30°C. Two strategies for increasing thethermostability of the enzyme are presented and discussed. Inthe first strategy, the solution thermodynamics of the systemis affected by osmolytes in such a way that heat-mediatedinactivation of the enzyme is prevented. In the secondstrategy, the enzyme is thermostabilized by mutagenesis. Bothstabilizing strategies can be utilized to allow bioluminometricassays to be performed at higher temperatures. For instance,both DNA polymerase and ATP sulfurylase activity could beanalyzed at 37°C.

The osmolyte strategy was successfully employed forincreasing the reaction temperature for the Pyrosequencingmethod. By increasing the reaction temperature to 37°Cunspecific signals from primer-dimers and 3’-end loopswere reduced. Furthermore, sequencing of a challenging templateat 37°C, which previously yielded poor, non-interpretablesequence signals at lower temperatures was now possible.

Introduction of a new adenosine nucleotide analog,7-deaza-2’-deoxyadenosine-5’-triphosphate (c7dATP) reduced the inhibitory effect on apyraseobserved with the currently used analog,2’-deoxyadenosine-5’-O-(1-thiotriphosphate)(dATPαS).

Sequencing of homopolymeric T-regions has previously beendifficult with the exonuclease-deficient form of the DNApolymerase I large (Klenow) fragment. By using the DNApolymerase from bacteriophage T7, known as Sequenase, templateswith homopolymeric T-regions were successfully sequenced.Furthermore, it was found that the strand displacement activityfor both polymerases was strongly assisted if the displacedstrand had a 5’-overhang. In contrast, the stranddisplacement activity for both polymerases was inhibitedwithout an overhang, resulting in reduced sequencingperformance in double stranded regions.

A firefly bioluminescent assay for the real-time detectionof inorganic pyrophosphatase in the hydrolytic direction wasalso developed. The assay is versatile and has a linearresponse in the range between 8 and 500 mU.

Key words:bioluminescence, osmolytes, glycine betaine,thermostability, firefly luciferase, inorganic pyrophosphatase,inorganic pyrophosphate, Pyrosequencing technology, secondaryDNA-structures, Sequenase, Klenow-polymerase, reaction rates,temperature, c7dATP, dATPαS.

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Books on the topic "Luciferasi"

1

A, DeLuca Marlene, and McElroy William David 1917-, eds. Bioluminescence and chemiluminescence. Orlando: Academic Press, 1986.

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M, Ziegler Miriam, and Baldwin Thomas O, eds. Bioluminescence and chemiluminescence. San Diego, Calif: Academic Press, 2000.

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Thompson, James. Lucifer's tears. London: Avon, 2011.

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Rollins, L. A. Lucifer's lexicon. Port Townsend, Wash: Loompanics Unlimited, 1987.

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Cave, Hugh B. Lucifer's eye. New York: Tom Doherty, 1991.

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Larry, Niven. Lucifer's hammer. New York: Ballantine Pub. Group, 1998.

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Lucifer's tears. Waterville, Me: Thorndike Press, 2011.

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Lucifer's crown. Waterville, Me: Five Star, 2004.

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Lucifer's lady. London: Hale, 1988.

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Lucifer's flood. Lake Mary, Fla: Realms, 2008.

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Book chapters on the topic "Luciferasi"

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Deluca, Marlene. "Firefly Luciferase." In Advances in Enzymology - and Related Areas of Molecular Biology, 37–68. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122891.ch2.

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Wettey, Frank R., and Antony P. Jackson. "Luciferase reporter assay." In Subcellular Biochemistry, 423–25. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/978-1-4020-4896-8_39.

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Arndt, T. "Luciferin-Luciferase-System." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_1977-1.

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Arndt, T. "Luciferin-Luciferase-System." In Springer Reference Medizin, 1535. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1977.

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Bauer, Paul. "Luciferase Reporter Gene Assays." In Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_3430-2.

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Barry, Michael A., Shannon May, and Eric A. Weaver. "Imaging Luciferase-Expressing Viruses." In Methods in Molecular Biology, 79–87. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-340-0_6.

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McClung, C. Robertson, and Qiguang Xie. "Measurement of Luciferase Rhythms." In Methods in Molecular Biology, 1–11. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0700-7_1.

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Bauer, Paul. "Luciferase Reporter Gene Assays." In Encyclopedia of Cancer, 2543–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_3430.

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Bauer, Paul. "Luciferase Reporter Gene Assays." In Encyclopedia of Cancer, 2077–81. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_3430.

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Sarrion-Perdigones, Alejandro, Yezabel Gonzalez, Lyra Chang, Tatiana Gallego-Flores, Damian W. Young, and Koen J. T. Venken. "Multiplex Hextuple Luciferase Assaying." In Bioluminescence, 433–56. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2453-1_33.

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Conference papers on the topic "Luciferasi"

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HOSSEINKHANI, SAMAN, NARGES KH TAFRESHI, MAJID SADEGHIZADEH, RAHMAN EMAMZADEH, BIJAN RANJBAR, and HOSSEIN NADERI-MANESH. "SITE-DIRECTED MUTAGENESIS OF LAMPYRIS TURKESTANICUS LUCIFERASE: THE EFFECT OF CONSERVED RESIDUE(S) IN BIOLUMINESCENCE EMISSION SPECTRA AMONG FIREFLY LUCIFERASES." In Proceedings of the 15th International Symposium. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812839589_0004.

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Fan, Z. Hugh, Qian Mei, and Steve Soper. "Microfluidic Reactors for Bioluminescence Detection." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-12464.

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Bioluminescence detection is often achieved by using luciferase as an enzyme. When it is implemented in a microfluidic device, the enzyme must be properly mixed with luciferase assay reagents (LAR) to achieve enzymatic reactions. Two microfluidic reactors are investigated in this work for bioluminescence detection. The reactors were fabricated in poly(methylmethacrylate), PMMA, by hot embossing using a mold master with the reactor layouts made by high-precision micromilling. Reactor I device contains staggered herringbone mixers. Reactor II device has the same layout except that the mixers were replaced with smooth channels. We found that the mixing efficiency in Reactor I was 17.8 times higher than Reactor II. Theoretical analysis of the experimental results indicated that the required channel length of mixing was linearly proportional to the flow rate. A calibration curve for luciferase was obtained for both reactors. The limit of detection in Reactor I was determined to be 0.14 μg/mL of luciferase.
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MEZHEVIKIN, VV, IE SUKOVATAYA, and NA TYULKOVA. "KINETIC INVESTIGATION OF BACTERIAL LUCIFERASE." In Proceedings of the 13th International Symposium. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702203_0018.

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SZITTNER, ROSE, LEO LIN, and EDWARD MEIGHEN. "CHIMERIC BACTERIAL LUCIFERASES." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0033.

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UGAROVA, N. N., E. I. DEMENTIEVA, and I. A. LUNDOVSKIKH. "THERMOINACTIVATION AND REACTIVATION OF FIREFLY LUCIFERASE." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0048.

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LAW, G. H., O. A. GANDELMAN, L. C. TISI, C. R. LOWE, and JAH MURRAY. "ALTERING THE SURFACE HYDROPHOBICITY OF FIREFLY LUCIFERASE." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0007.

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Kuhn, Jonathan, Rachel Broza, and Ekaterina Verkin. "Making temporal maps using bacterial luciferase: Bacteriophage." In Biomedical Optics 2004, edited by Alexander P. Savitsky, Lubov Y. Brovko, Darryl J. Bornhop, Ramesh Raghavachari, and Samuel I. Achilefu. SPIE, 2004. http://dx.doi.org/10.1117/12.530706.

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HAWKINS, E. M., D. GARVIN, A. PAGUIO, P. STECHA, B. SWANSON, F. FAN, and K. V. WOOD. "ADVANCING THE DEVELOPMENT OF DUAL-LUCIFERASE ASSAYS." In Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0024.

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JATHOUL, A. P., O. A. GANDELMAN, G. H. E. LAW, J. A. H. MURRAY, and L. C. TISI. "DESIGNING ENHANCED THERMOSTABLE LUCIFERASE FOR PROTEOLYTIC ASSAY." In Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0026.

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ZHUANG, YAO, AILEEN P. PAGUIO, MONIKA G. GRUBER, and KEITH V. WOOD. "SYNTHETIC LUCIFERASE GENES AS BETTER REPORTER MOLECULES." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0114.

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Reports on the topic "Luciferasi"

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McElroy, W. D. Firefly Luciferase-Structure and Function. Fort Belvoir, VA: Defense Technical Information Center, July 1988. http://dx.doi.org/10.21236/ada198292.

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Wu, Anna M. F-18 Labeled Diabody-Luciferase Fusion Proteins for Optical-ImmunoPET. Office of Scientific and Technical Information (OSTI), January 2013. http://dx.doi.org/10.2172/1060194.

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Wood, Keith V. Luciferases of Luminous Beetles: Evolution, Color Variation, and Applications. Fort Belvoir, VA: Defense Technical Information Center, March 1992. http://dx.doi.org/10.21236/ada251122.

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Iglesia-Rodriguez, M. D., Oscar M. Schofield, Scott M. Glenn, and Mark Moline. Development of a Suite of Luciferase Gene Probes for the Screening and Detection of Marine Bioluminescent Systems and Organisms. Fort Belvoir, VA: Defense Technical Information Center, January 2006. http://dx.doi.org/10.21236/ada523730.

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Iglesia-Rodriguez, M. D., Oscar M. Schofield, Scott M. Glenn, and Mark Moline. Development of a Suite of Luciferase Gene Probes for the Screening and Detection of Marine Bioluminescent Systems and Organisms. Fort Belvoir, VA: Defense Technical Information Center, September 2007. http://dx.doi.org/10.21236/ada550656.

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Locy, Robert D., Hillel Fromm, Joe H. Cherry, and Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, January 2001. http://dx.doi.org/10.32747/2001.7575288.bard.

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Most plants accumulate the nonprotein amino acid, g-aminobutyric acid (GABA), in response to heat stress. GABA is made from glutamate in a reaction catalyzed by glutamate decarboxylase (GAD), an enzyme that has been shown by the Israeli PI to be a calmodulin (CaM) binding protein whose activity is regulated in vitro by calcium and CaM. In Arabidopsis there are at least 5 GAD genes, two isoforms of GAD, GAD1 and GAD2, are known to be expressed, both of which appear to be calmodulin-binding proteins. The role of GABA accumulation in stress tolerance remains unclear, and thus the objectives of the proposed work are intended to clarify the possible roles of GABA in stress tolerance by studying the factors which regulate the activity of GAD in vivo. Our intent was to demonstrate the factors that mediate the expression of GAD activity by analyzing the promoters of the GAD1 and GAD2 genes, to determine the role of stress induced calcium signaling in the regulation of GAD activity, to investigate the role of phosphorylation of the CaM-binding domain in the regulation of GAD activity, and to investigate whether ABA signaling could be involved in GAD regulation via the following set of original Project Objectives: 1. Construction of chimeric GAD1 and GAD2 promoter/reporter gene fusions and their utilization for determining cell-specific expression of GAD genes in Arabidopsis. 2. Utilizing transgenic plants harboring chimeric GAD1 promoter-luciferase constructs for isolating mutants in genes controlling GAD1 gene activation in response to heat shock. 3. Assess the role of Ca2+/CaM in the regulation of GAD activity in vivo in Arabidopsis. 4. Study the possible phosphorylation of GAD as a means of regulation of GAD activity. 5. Utilize ABA mutants of Arabidopsis to assess the involvement of this phytohormone in GAD activation by stress stimuli. The major conclusions of Objective 1 was that GAD1 was strongly expressed in the elongating region of the root, while GAD2 was mainly expressed along the phloem in both roots and shoots. In addition, GAD activity was found not to be transcriptionally regulated in response to heat stress. Subsequently, The Israeli side obtained a GAD1 knockout mutation, and in light of the objective 1 results it was determined that characterization of this knockout mutation would contribute more to the project than the proposed Objective 2. The major conclusion of Objective 3 is that heat-stress-induced changes in GAD activity can be explained by heat-stress-induced changes in cytosolic calcium levels. No evidence that GAD activity was transcriptionally or translationally regulated or that protein phosphorylation was involved in GAD regulation (objective 4) was obtained. Previously published data by others showing that in wheat roots ABA regulated GABA accumulation proved not to be the case in Arabidopsis (Objective 5). Consequently, we put the remaining effort in the project into the selection of mutants related to temperature adaptation and GABA utilization and attempting to characterize events resulting from GABA accumulation. A set of 3 heat sensitive mutants that appear to have GABA related mutations have been isolated and partially characterized, and a study linking GABA accumulation to growth stimulation and altered nitrate assimilation were conducted. By providing a better understanding of how GAD activity was and was not regulated in vivo, we have ruled out the use of certain genes for genetically engineering thermotolerance, and suggested other areas of endeavor related to the thrust of the project that may be more likely approaches to genetically engineering thermotolerance.
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Sessa, Guido, and Gregory Martin. MAP kinase cascades activated by SlMAPKKKε and their involvement in tomato resistance to bacterial pathogens. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7699834.bard.

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The research problem: Pseudomonas syringae pv. tomato (Pst) and Xanthomonas campestrispv. vesicatoria (Xcv) are the causal agents of tomato bacterial speck and spot diseases, respectively. These pathogens colonize the aerial parts of the plant and cause economically important losses to tomato yield worldwide. Control of speck and spot diseases by cultural practices or chemicals is not effective and genetic sources of resistance are very limited. In previous research supported by BARD, by gene expression profiling we identified signaling components involved in resistance to Xcvstrains. Follow up experiments revealed that a tomato gene encoding a MAP kinase kinase kinase (MAPKKKe) is required for resistance to Xcvand Pststrains. Goals: Central goal of this research was to investigate the molecular mechanisms by which MAPKKKεand associated MAP kinase cascades regulate host resistance. Specific objectives were to: 1. Determine whether MAPKKKεplays a broad role in defense signaling in plants; 2. Identify components of MAP kinase cascades acting downstream of MAPKKKε; 3. Determine the role of phosphorylation-related events in the function of MAPKKKε; 4. Isolate proteins directly activated by MAPKKKε-associatedMAPK modules. Our main achievements during this research program are in the following major areas: 1. Characterization of MAPKKKεas a positive regulator of cell death and dissection of downstream MAP kinase cascades (Melech-Bonfil et al., 2010; Melech-Bonfil and Sessa, 2011). The MAPKKKεgene was found to be required for tomato resistance to Xcvand Pstbacterial strains and for hypersensitive response cell death triggered by different R gene/effector gene pairs. In addition, overexpression analysis demonstrated that MAPKKKεis a positive regulator of cell death, whose activity depends on an intact kinase catalytic domain. Epistatic experiments delineated a signaling cascade downstream of MAPKKKεand identified SIPKK as a negative regulator of MAPKKKε-mediated cell death. Finally, genes encoding MAP kinase components downstream of MAPKKKεwere shown to contribute to tomato resistance to Xcv. 2. Identification of tomato proteins that interact with MAPKKKεand play a role in plant immunity (Oh et al., 2011). We identified proteins that interact with MAPKKKε. Among them, the 14-3-3 protein TFT7 was required for cell death mediated by several R proteins. In addition, TFT7 interacted with the MAPKK SlMKK2 and formed homodimersin vivo. Thus, TFT7 is proposed to recruit SlMKK2 and MAPKKK client proteins for efficient signal transfer. 3. Development of a chemical genetic approach to identify substrates of MAPKKKε-activated MAP kinase cascades (Salomon et al., 2009, 2011). This approach is based on engineering the kinase of interest to accept unnatural ATP analogs. For its implementation to identify substrates of MAPKKKε-activated MAP kinase modules, we sensitized the tomato MAP kinase SlMPK3 to ATP analogs and verified its ability to use them as phosphodonors. By using the sensitized SlMPK3 and radiolabeled N6(benzyl)ATP it should be possible to tag direct substrates of this kinase. 4. Development of methods to study immunity triggered by pathogen-associated molecular patterns (PAMPs) in tomato and N. benthamiana plants (Kim et al., 2009; Nguyen et al. 2010). We developed protocols for measuring various PTI-associatedphenotypes, including bacterial populations after pretreatment of leaves with PAMPs, induction of reporter genes, callose deposition at the cell wall, activation of MAP kinases, and a luciferase-based reporter system for use in protoplasts. Scientific and agricultural significance: Our research activities discovered and characterized a signal transduction pathway mediating plant immunity to bacterial pathogens. Increased understanding of molecular mechanisms of immunity will allow them to be manipulated by both molecular breeding and genetic engineering to produce plants with enhanced natural defense against disease. In addition, we successfully developed new biochemical and molecular methods that can be implemented in the study of plant immunity and other aspects of plant biology.
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Schwartz, Bertha, Vaclav Vetvicka, Ofer Danai, and Yitzhak Hadar. Increasing the value of mushrooms as functional foods: induction of alpha and beta glucan content via novel cultivation methods. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7600033.bard.

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During the granting period, we performed the following projects: Firstly, we differentially measured glucan content in several pleurotus mushroom strains. Mushroom polysaccharides are edible polymers that have numerous reported biological functions; the most common effects are attributed to β-glucans. In recent years, it became apparent that the less abundant α-glucans also possess potent effects in various health conditions. In our first study, we explored several Pleurotus species for their total, β and α-glucan content. Pleurotuseryngii was found to have the highest total glucan concentrations and the highest α-glucans proportion. We also found that the stalks (stipe) of the fruit body contained higher glucan content then the caps (pileus). Since mushrooms respond markedly to changes in environmental and growth conditions, we developed cultivation methods aiming to increase the levels of α and β-glucans. Using olive mill solid waste (OMSW) from three-phase olive mills in the cultivation substrate. We were able to enrich the levels mainly of α-glucans. Maximal total glucan concentrations were enhanced up to twice when the growth substrate contained 80% of OMSW compared to no OMSW. Taking together this study demonstrate that Pleurotuseryngii can serve as a potential rich source of glucans for nutritional and medicinal applications and that glucan content in mushroom fruiting bodies can be further enriched by applying OMSW into the cultivation substrate. We then compared the immune-modulating activity of glucans extracted from P. ostreatus and P. eryngii on phagocytosis of peripheral blood neutrophils, and superoxide release from HL-60 cells. The results suggest that the anti-inflammatory properties of these glucans are partially mediated through modulation of neutrophileffector functions (P. eryngiiwas more effective). Additionally, both glucans dose-dependently competed for the anti-Dectin-1 and anti-CR3 antibody binding. We then tested the putative anti-inflammatory effects of the extracted glucans in inflammatory bowel disease (IBD) using the dextran sulfate sodium (DSS)–induced model in mice. The clinical symptoms of IBD were efficiently relieved by the treatment with two different doses of the glucan from both fungi. Glucan fractions, from either P. ostreatus or P. eryngii, markedly prevented TNF-α mediated inflammation in the DSS–induced inflamed intestine. These results suggest that there are variations in glucan preparations from different fungi in their anti-inflammatory ability. In our next study, we tested the effect of glucans on lipopolysaccharide (LPS)-induced production of TNF-α. We demonstrated that glucan extracts are more effective than mill mushroom preparations. Additionally, the effectiveness of stalk-derived glucans were slightly more pronounced than of caps. Cap and stalk glucans from mill or isolated glucan competed dose-dependently with anti-Dectin-and anti-CR-3 antibodies, indicating that they contain β-glucans recognized by these receptors. Using the dextran sulfate sodium (DSS)-inflammatory bowel disease mice model, intestinal inflammatory response to the mill preparations was measured and compared to extracted glucan fractions from caps and stalks. We found that mill and glucan extracts were very effective in downregulatingIFN-γ and MIP-2 levels and that stalk-derived preparations were more effective than from caps. The tested glucans were equally effective in regulating the number of CD14/CD16 monocytes and upregulating the levels of fecal-released IgA to almost normal levels. In conclusion, the most effective glucans in ameliorating some IBD-inflammatory associated symptoms induced by DSS treatment in mice were glucan extracts prepared from the stalk of P. eryngii. These spatial distinctions may be helpful in selecting more effective specific anti-inflammatory mushrooms-derived glucans. We additionally tested the effect of glucans on lipopolysaccharide-induced production of TNF-α, which demonstrated stalk-derived glucans were more effective than of caps-derived glucans. Isolated glucans competed with anti-Dectin-1 and anti-CR3 antibodies, indicating that they contain β-glucans recognized by these receptors. In conclusion, the most effective glucans in ameliorating IBD-associated symptoms induced by DSS treatment in mice were glucan extracts prepared from the stalk of P. eryngii grown at higher concentrations of OMSW. We conclude that these stress-induced growing conditions may be helpful in selecting more effective glucans derived from edible mushrooms. Based on the findings that we could enhance glucan content in Pleurotuseryngii following cultivation of the mushrooms on a substrate containing different concentrations of olive mill solid waste (OMSW) and that these changes are directly related to the content of OMSW in the growing substrate we tested the extracted glucans in several models. Using dextran sulfate sodium (DSS)–inflammatory bowel disease (IBD) mice model, we measured the colonic inflammatory response to the different glucan preparations. We found that the histology damaging score (HDS) resulting from DSS treatment reach a value of 11.8 ± 2.3 were efficiently downregulated by treatment with the fungal extracted glucans, glucans extracted from stalks cultivated at 20% OMSWdownregulated to a HDS value of 6.4 ± 0.5 and at 80% OMSW showed the strongest effects (5.5 ± 0.6). Similar downregulatory effects were obtained for expression of various intestinal cytokines. All tested glucans were equally effective in regulating the number of CD14/CD16 monocytes from 18.2 ± 2.7 % for DSS to 6.4 ± 2.0 for DSS +glucans extracted from stalks cultivated at 50% OMSW. We finally tested glucans extracted from Pleurotuseryngii grown on a substrate containing increasing concentrations of olive mill solid waste (OMSW) contain greater glucan concentrations as a function of OMSW content. Treatment of rat Intestinal epithelial cells (IEC-6) transiently transfected with Nf-κB fused to luciferase demonstrated that glucans extracted from P. eryngii stalks grown on 80% OMSWdownregulatedTNF-α activation. Glucans from mushrooms grown on 80% OMSW exerted the most significant reducing activity of nitric oxide production in lipopolysaccharide (LPS) treated J774A.1 murine macrophages. The isolated glucans were tested in vivo using the Dextran Sodium Sulfate (DSS) induced colitis in C57Bl/6 mice and found to reduce the histology damaging score resulting from DSS treatment. Expression of various intestinal cytokines were efficiently downregulated by treatment with the fungal extracted glucans. We conclude that the stress-induced growing conditions exerted by OMSW induces production of more effective anti-inflammatory glucans in P. eryngii stalks.
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Replenishing the malaria drug discovery pipeline: Screening and hit evaluation of the MMV Hit Generation Library 1 (HGL1) against asexual blood stage Plasmodium falciparum using a nano luciferase reporter read-out. EMBL-EBI, August 2022. http://dx.doi.org/10.6019/chembl4888484.

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