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Journal articles on the topic 'Trehalase inhibitors'

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Published: 9 March 2023

Last updated: 10 March 2023

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1

White, Christopher, Deborah B. Lee, and Stephen J. Free. "NEUROSPORA TREHALASE AND ITS STRUCTURAL GENE." Genetics 110, no. 2 (June 1, 1985): 217–27. http://dx.doi.org/10.1093/genetics/110.2.217.

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ABSTRACT We have isolated Neurospora trehalaseless mutants and mapped the trehalase structural gene to linkage group I. The structural gene mutations not only affect thermostability and other characteristics of the enzyme but also affect the production of an inhibitor of the wild-type trehalase. The inhibitor appears to be the mutant trehalase. We suggest that the mutant subunits act as inhibitors by entering into the multimeric forms of the enzyme and altering the ability of the normal wild-type subunits to catalyze the cleavage of trehalose.—Wild type trehalase has been purified to near homogeneity, and its characteristics have been studied. It was purified as a tetramer, with each subunit having a molecular weight of 88,000.—We have studied the regulation of trehalase and found the production of trehalase to be glucose repressible. Cells begin to produce trehalase 60 min after being transferred to glucose-free medium.

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2

Matassini, Camilla, Camilla Parmeggiani, and Francesca Cardona. "New Frontiers on Human Safe Insecticides and Fungicides: An Opinion on Trehalase Inhibitors." Molecules 25, no. 13 (July 1, 2020): 3013. http://dx.doi.org/10.3390/molecules25133013.

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In the era of green economy, trehalase inhibitors represent a valuable chance to develop non-toxic pesticides, being hydrophilic compounds that do not persist in the environment. The lesson on this topic that we learned from the past can be of great help in the research on new specific green pesticides. This review aims to describe the efforts made in the last 50 years in the evaluation of natural compounds and their analogues as trehalase inhibitors, in view of their potential use as insecticides and fungicides. Specifically, we analyzed trehalase inhibitors based on sugars and sugar mimics, focusing on those showing good inhibition properties towards insect trehalases. Despite their attractiveness as a target, up to now there are no trehalase inhibitors that have been developed as commercial insecticides. Although natural complex pseudo di- and trisaccharides were firstly studied to this aim, iminosugars look to be more promising, showing an excellent specificity profile towards insect trehalases. The results reported here represent an overview and a discussion of the best candidates which may lead to the development of an effective insecticide in the future.

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3

Marten, Andrew D., Alicyn I. Stothard, Karishma Kalera, Benjamin M. Swarts, and Michael J. Conway. "Validamycin A Delays Development and Prevents Flight in Aedes aegypti (Diptera: Culicidae)." Journal of Medical Entomology 57, no. 4 (January 26, 2020): 1096–103. http://dx.doi.org/10.1093/jme/tjaa004.

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Abstract Trehalose is a disaccharide that is the major sugar found in insect hemolymph fluid. Trehalose provides energy, and promotes growth, metamorphosis, stress recovery, chitin synthesis, and insect flight. The hydrolysis of trehalose is under the enzymatic control of the enzyme trehalase. Trehalase is critical to the role of trehalose in insect physiology, and is required for the regulation of metabolism and glucose generation. Trehalase inhibitors represent a novel class of insecticides that have not been fully developed. Here, we tested the ability of trehalose analogues to function as larvacides or adulticides in an important disease vector—Aedes aegypti. We show that validamycin A, but not 5-thiotrehalose, delays larval and pupal development and prevents flight of adult mosquitoes. Larval mosquitoes treated with validamycin A were hypoglycemic and pupae had increased levels of trehalose. Treatment also skewed the sex ratio toward male mosquitoes. These data reveal that validamycin A is a mosquito adulticide that can impair normal development of an important disease vector.

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4

Streeter, J. G., and M. L. Gomez. "Three Enzymes for Trehalose Synthesis in Bradyrhizobium Cultured Bacteria and in Bacteroids from Soybean Nodules." Applied and Environmental Microbiology 72, no. 6 (June 2006): 4250–55. http://dx.doi.org/10.1128/aem.00256-06.

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ABSTRACT α,α-Trehalose is a disaccharide accumulated by many microorganisms, including rhizobia, and a common role for trehalose is protection of membrane and protein structure during periods of stress, such as desiccation. Cultured Bradyrhizobium japonicum and B. elkanii were found to have three enzymes for trehalose synthesis: trehalose synthase (TS), maltooligosyltrehalose synthase (MOTS), and trehalose-6-phosphate synthetase. The activity level of the latter enzyme was much higher than those of the other two in cultured bacteria, but the reverse was true in bacteroids from nodules. Although TS was the dominant enzyme in bacteroids, the source of maltose, the substrate for TS, is not clear; i.e., the maltose concentration in nodules was very low and no maltose was formed by bacteroid protein preparations from maltooligosaccharides. Because bacteroid protein preparations contained high trehalase activity, it was imperative to inhibit this enzyme in studies of TS and MOTS in bacteroids. Validamycin A, a commonly used trehalase inhibitor, was found to also inhibit TS and MOTS, and other trehalase inhibitors, such as trehazolin, must be used in studies of these enzymes in nodules. The results of a survey of five other species of rhizobia indicated that most species sampled had only one major mechanism for trehalose synthesis. The presence of three totally independent mechanisms for the synthesis of trehalose by Bradyrhizobium species suggests that this disaccharide is important in the function of this organism both in the free-living state and in symbiosis.

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5

KAMEDA, YUKIHIKO, NAOKI ASANO, TAKUJI YAMAGUCHI, and KATSUHIKO MATSUI. "Validoxylamines as trehalase inhibitors." Journal of Antibiotics 40, no. 4 (1987): 563–65. http://dx.doi.org/10.7164/antibiotics.40.563.

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6

Bini, Davide, Francesca Cardona, Matilde Forcella, Camilla Parmeggiani, Paolo Parenti, Francesco Nicotra, and Laura Cipolla. "Synthesis and biological evaluation of nojirimycin- and pyrrolidine-based trehalase inhibitors." Beilstein Journal of Organic Chemistry 8 (April 5, 2012): 514–21. http://dx.doi.org/10.3762/bjoc.8.58.

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A small set of nojirimycin- and pyrrolidine-based iminosugar derivatives has been synthesized and evaluated as potential inhibitors of porcine and insect trehalases. Compounds 12, 13 and 20 proved to be active against both insect and porcine trehalases with selectivity towards the insect glycosidase, while compounds 10, 14 and 16 behaved as inhibitors only of insect trehalase. Despite the fact that the activity was found in the micromolar range, these findings may help in elucidating the structural features of this class of enzymes of different origin, which are still scarcely characterised.

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7

Kyosseva, S. V., Z. N. Kyossev, and A. D. Elbein. "Inhibitors of Pig Kidney Trehalase." Archives of Biochemistry and Biophysics 316, no. 2 (February 1995): 821–26. http://dx.doi.org/10.1006/abbi.1995.1110.

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8

QIAN, XUHONG, ZHIBIN LI, ZHI LIU, GONGHUA SONG, and ZHONG LI. "Syntheses of 2-Aryliminooxazolidine Derivatives as Trehalase Inhibitors." Journal of Antibiotics 54, no. 12 (2001): 1108–10. http://dx.doi.org/10.7164/antibiotics.54.1108.

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9

Gibson, Robert P, Tracey M Gloster, Shirley Roberts, R. Anthony J Warren, Isabel Storch de Gracia, Ángela García, Jose L Chiara, and Gideon J Davies. "Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors." Angewandte Chemie 119, no. 22 (May 25, 2007): 4193–97. http://dx.doi.org/10.1002/ange.200604825.

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10

Gibson, Robert P, Tracey M Gloster, Shirley Roberts, R. Anthony J Warren, Isabel Storch de Gracia, Ángela García, Jose L Chiara, and Gideon J Davies. "Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors." Angewandte Chemie International Edition 46, no. 22 (May 25, 2007): 4115–19. http://dx.doi.org/10.1002/anie.200604825.

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11

ASANO, NAOKI, MASAYOSHI TAKEUCHI, YUKIHIKO KAMEDA, KATSUHIKO MATSUI, and YOSHIAKI KONO. "Trehalase inhibitors, validoxylamine A and related compounds as insecticides." Journal of Antibiotics 43, no. 6 (1990): 722–26. http://dx.doi.org/10.7164/antibiotics.43.722.

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12

Cipolla, Laura, Antonella Sgambato, Matilde Forcella, Paola Fusi, Paolo Parenti, Francesca Cardona, and Davide Bini. "N-Bridged 1-deoxynojirimycin dimers as selective insect trehalase inhibitors." Carbohydrate Research 389 (May 2014): 46–49. http://dx.doi.org/10.1016/j.carres.2013.12.025.

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13

Qian, Xuhong, Zhibin Li, Zhi Liu, Gonghua Song, and Zhong Li. "ChemInform Abstract: Syntheses of 2-Aryliminooxazolidine Derivatives as Trehalase Inhibitors." ChemInform 33, no. 22 (May 21, 2010): no. http://dx.doi.org/10.1002/chin.200222126.

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14

Bansal, Raman, M. A. Rouf Mian, Omprakash Mittapalli, and Andy P. Michel. "Molecular characterization and expression analysis of soluble trehalase gene in Aphis glycines, a migratory pest of soybean." Bulletin of Entomological Research 103, no. 3 (February 28, 2013): 286–95. http://dx.doi.org/10.1017/s0007485312000697.

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AbstractIn insects, the enzyme trehalase plays a crucial role in energy metabolism, chitin synthesis and possibly during plant–insect interactions. We have characterized a soluble trehalase gene (Tre-1) from cDNA of Aphis glycines, a serious migratory pest of soybean. The full-length cDNA of Tre-1 in A. glycines (AyTre-1) was 2550 bp long with an open reading frame of 1770 bp that encoded for a 589 amino acid residues protein. Sequence assessment and phylogenetic analysis of the putative protein suggested that the selected cDNA belongs to soluble trehalase group. Quantitative PCR (qPCR) analysis in different tissues and developmental stages revealed peak mRNA levels of AyTre-1 in the gut (compared with other tissues assayed) and highest expression in the second instar compared with the other developmental stages assayed. Interestingly, a significantly increased expression of AyTre-1 (1.9-fold, P < 0.05) was observed in the alate morphs compared with that in apterate morphs. However, there was no significant difference in AyTre-1 expression in A. glycines-nymphs fed with resistant and susceptible plants. Expression patterns identified in this study provide a platform to investigate the role of AyTre-1 in physiological activities such as flight and feeding in A. glycines. The characterization of soluble trehalase gene may help to develop novel strategies to manage A. glycines using trehalase inhibitors and using RNA interference for knock-down of AyTre-1 expression.

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15

Chen, C. C., W. J. Guo, and K. J. Isselbacher. "Rat intestinal trehalase. Studies of the active site." Biochemical Journal 247, no. 3 (November 1, 1987): 715–24. http://dx.doi.org/10.1042/bj2470715.

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Rat intestinal trehalase was solubilized, purified and reconstituted into proteoliposomes. With octyl glucoside as the solubilizing detergent, the purified protein appeared as a single band on SDS/polyacrylamide-gel electrophoresis with an apparent molecular mass of 67 kDa. Kinetic studies indicated that the active site of this enzyme can be functionally divided into two adjacent regions, namely a binding site (with pKa 4.8) and a catalytic site (with pKa 7.2). Other findings suggested that the catalytic site contains a functional thiol group, which is sensitive to inhibition by N-ethylmaleimide, Hg2+ and iodoacetate. Substrate protection and iodoacetate labelling of the thiol group demonstrated that only a protein of 67 kDa was labelled. Furthermore, sucrose and phlorizin protected the thiol group, but Tris-like inhibitors did not. Structure-inhibition analysis of Tris-like inhibitors, the pH effect of Tris inhibition and Tris protection of 1-(3-dimethylaminopropyl)-3-ethylcarbodi-imide inactivation permitted characterization and location of a separate site containing a carboxy group for Tris binding, which may also be the binding region. On the basis of these findings, a possible structure for the active site of trehalase is proposed.

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16

Ogawa, Seiichiro, Chikara Uchida, and Yu Yuming. "Synthesis of aminocyclitol moieties of trehalase inhibitors, trehalostatin and trehazolin. Correct structure of the inhibitor." Journal of the Chemical Society, Chemical Communications, no. 12 (1992): 886. http://dx.doi.org/10.1039/c39920000886.

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17

Fernandez, J., T. Soto, J. Vicente-Soler, J. Cansado, and M. Gacto. "Trehalase activation induced by nutrients and metabolic inhibitors in Zygosaccharomyces rouxii." Mycological Research 100, no. 12 (January 1996): 1440–44. http://dx.doi.org/10.1016/s0953-7562(96)80075-x.

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18

Bini, Davide, Matilde Forcella, Laura Cipolla, Paola Fusi, Camilla Matassini, and Francesca Cardona. "Synthesis of Novel Iminosugar-Based Trehalase Inhibitors by Cross-Metathesis Reactions." European Journal of Organic Chemistry 2011, no. 20-21 (June 1, 2011): 3995–4000. http://dx.doi.org/10.1002/ejoc.201100484.

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19

El Nemr, Ahmed, and El Sayed H. El Ashry. "ChemInform Abstract: Potential Trehalase Inhibitors: Syntheses of Trehazolin and Its Analogues." ChemInform 43, no. 4 (December 29, 2011): no. http://dx.doi.org/10.1002/chin.201204254.

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20

Cendret, V., T. Legigan, A. Mingot, S. Thibaudeau, I. Adachi, M. Forcella, P. Parenti, et al. "Synthetic deoxynojirimycin derivatives bearing a thiolated, fluorinated or unsaturated N-alkyl chain: identification of potent α-glucosidase and trehalase inhibitors as well as F508del-CFTR correctors." Organic & Biomolecular Chemistry 13, no. 43 (2015): 10734–44. http://dx.doi.org/10.1039/c5ob01526j.

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21

Adedeji, Eunice O., Gbolahan O. Oduselu, Olubanke O. Ogunlana, Segun Fatumo, Rainer Koenig, and Ezekiel Adebiyi. "Anopheles gambiae Trehalase Inhibitors for Malaria Vector Control: A Molecular Docking and Molecular Dynamics Study." Insects 13, no. 11 (November 19, 2022): 1070. http://dx.doi.org/10.3390/insects13111070.

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Trehalase inhibitors are considered safe alternatives for insecticides and fungicides. However, there are no studies testing these compounds on Anopheles gambiae, a major vector of human malaria. This study predicted the three-dimensional structure of Anopheles gambiae trehalase (AgTre) and identified potential inhibitors using molecular docking and molecular dynamics methods. Robetta server, C-I-TASSER, and I-TASSER were used to predict the protein structure, while the structural assessment was carried out using SWISS-MODEL, ERRAT, and VERIFY3D. Molecular docking and screening of 3022 compounds was carried out using AutoDock Vina in PyRx, and MD simulation was carried out using NAMD. The Robetta model outperformed all other models and was used for docking and simulation studies. After a post-screening analysis and ADMET studies, uniflorine, 67837201, 10406567, and Compound 2 were considered the best hits with binding energies of −6.9, −8.9, −9, and −8.4 kcal/mol, respectively, better than validamycin A standard (−5.4 kcal/mol). These four compounds were predicted to have no eco-toxicity, Brenk, or PAINS alerts. Similarly, they were predicted to be non-mutagenic, carcinogenic, or hepatoxic. 67837201, 10406567, and Compound 2 showed excellent stability during simulation. The study highlights uniflorine, 67837201, 10406567, and Compound 2 as good inhibitors of AgTre and possible compounds for malaria vector control.

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22

D'Adamio, Giampiero, Antonella Sgambato, Matilde Forcella, Silvia Caccia, Camilla Parmeggiani, Morena Casartelli, Paolo Parenti, et al. "New synthesis and biological evaluation of uniflorine A derivatives: towards specific insect trehalase inhibitors." Organic & Biomolecular Chemistry 13, no. 3 (2015): 886–92. http://dx.doi.org/10.1039/c4ob02016b.

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23

Tatun, Nujira, Tippawan Singtripop, Shingo Osugi, Siriluck Nachiangmai, Masafumi Iwami, and Sho Sakurai. "Possible involvement of proteinaceous and non-proteinaceous trehalase inhibitors in the regulation of hemolymph trehalose concentration in Bombyx mori." Applied Entomology and Zoology 44, no. 1 (2009): 85–94. http://dx.doi.org/10.1303/aez.2009.85.

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24

Qian, Xuhong, Zhibin Li, Zhi Liu, Gonghua Song, and Zhong Li. "Syntheses and activities as trehalase inhibitors of N-arylglycosylamines derived from fluorinated anilines." Carbohydrate Research 336, no. 1 (November 2001): 79–82. http://dx.doi.org/10.1016/s0008-6215(01)00126-4.

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25

Ogawa, Seiichiro, and Chikara Uchida. "Synthesis of aminocyclitol moieties of trehalase inhibitors, trehalostatin and trehazolin. Confirmation of the correct structure of the inhibitor." Journal of the Chemical Society, Perkin Transactions 1, no. 15 (1992): 1939. http://dx.doi.org/10.1039/p19920001939.

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26

Uchida, Chikara, Tatsuya Yamagishi, and Seiichiro Ogawa. "Total synthesis of the trehalase inhibitors trehalostatin and trehazolin, and of their diastereoisomers. Final structural confirmation of the inhibitor." Journal of the Chemical Society, Perkin Transactions 1, no. 5 (1994): 589. http://dx.doi.org/10.1039/p19940000589.

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27

Kanzaki, Hiroshi, Takafumi Nuhama, Akio Kobayashi, and Kazuyoshi Kawazu. "An Effective Method of Screening Glucose-rich Microbial Culture Filtrates for Insect Trehalase Inhibitors." Bioscience, Biotechnology, and Biochemistry 59, no. 3 (January 1995): 398–400. http://dx.doi.org/10.1271/bbb.59.398.

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28

OGAWA, S., and C. UCHIDA. "ChemInform Abstract: Synthesis of Aminocyclitol Moieties of Trehalase Inhibitors, Trehalostatin and Trehazolin. Confirmation of the Correct Structure of the Inhibitor." ChemInform 23, no. 49 (September 1, 2010): no. http://dx.doi.org/10.1002/chin.199249259.

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29

Qian, Xuhong, Zhibin Li, Zhi Liu, Gonghua Song, and Zhong Li. "ChemInform Abstract: Syntheses and Activities as Trehalase Inhibitors of N-Arylglycosylamines Derived from Fluorinated Anilines." ChemInform 33, no. 7 (May 22, 2010): no. http://dx.doi.org/10.1002/chin.200207217.

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30

Soto, Teresa, Juana Fernandez, Jero Vicente-Soler, Jose Cansado, and Mariano Gacto. "Posttranslational Regulatory Control of Trehalase Induced by Nutrients, Metabolic Inhibitors, and Physical Agents inPachysolen tannophilus." Fungal Genetics and Biology 20, no. 2 (June 1996): 143–51. http://dx.doi.org/10.1006/fgbi.1996.0029.

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31

UCHIDA, C., T. YAMAGISHI, and S. OGAWA. "ChemInform Abstract: Total Synthesis of the Trehalase Inhibitors Trehalostatin and Trehazolin, and of Their Diastereoisomers. Final Structural Confirmation of the Inhibitor." ChemInform 25, no. 27 (August 19, 2010): no. http://dx.doi.org/10.1002/chin.199427239.

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32

Park, No-Joong, Hee Kyung Lim, and In Taek Hwang. "An enhanced system to screen trehalase inhibitors using a microplate assay with a housefly enzyme source." Journal of Asia-Pacific Entomology 11, no. 3 (September 2008): 161–66. http://dx.doi.org/10.1016/j.aspen.2008.07.004.

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33

D’Adamio, Giampiero, Matilde Forcella, Paola Fusi, Paolo Parenti, Camilla Matassini, Xhenti Ferhati, Costanza Vanni, and Francesca Cardona. "Probing the Influence of Linker Length and Flexibility in the Design and Synthesis of New Trehalase Inhibitors." Molecules 23, no. 2 (February 16, 2018): 436. http://dx.doi.org/10.3390/molecules23020436.

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Qian, Xuhong, Zhi Liu, Zhibin Li, Zhong Li, and Gonghua Song. "Synthesis and Quantitative Structure−Activity Relationships of Fluorine-Containing 4,4-Dihydroxylmethyl-2-aryliminooxazo(thiazo)lidines as Trehalase Inhibitors." Journal of Agricultural and Food Chemistry 49, no. 11 (November 2001): 5279–84. http://dx.doi.org/10.1021/jf010632k.

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35

Basistha, Bipasha, Anil Kumar Ghosh, and Sumita Ghosh. "Regulation of trehalose metabolism by protein methylation in a mutant strain of Saccharomyces cerevisiae." NBU Journal of Plant Sciences 4, no. 1 (2010): 39–45. http://dx.doi.org/10.55734/nbujps.2010.v04i01.007.

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Trechaloseis a non reducing disaccharide occurring in a wide range of organisms, from bacteria, yeast, to lower and higher plants and insects. It is economically important as a potent stress protectant, protein and biological membrane stabilizer: hence biosynthesis of trchalose is an extremely important event. Regulation of trehalose metabolism by protein methylation has been reported from previous works of this laboratory. Trehalose metabolism was monitored during different stages of growth of Saccharomyces cerevisiae. HPLC and enzymatic determination of trehalose. glucose, trehalose 6 phosphate phosphatase TPP) and trehalose 6 phosphate synthase (TPS) were carried out. It was noticed that trchalose, glucose TPP and TPS pcaked at Aso20 during growth but during this period the hydrolyzing enzymes, acid trehalase (AT) and neutral trehalase (NT) are found to be low. Effect of a potent universal methyl group donor S-adenosyl-L-methionine (AdoMet), and a methylation inhibitor, oxidized adenosine (Adox) on trehalose metabolism has been studied. Trehalose metabolism is altered when YPD grown cells were incubated for I hr in presence of cither 1 mM Adox or AdoMet at 30'C and pH 6.0 TPS showed a slight increase in specific activity in cells incubated with AdoMet over Adox. Trehalose level of Adox treated cells were seen to be lower than control throughout the period of incubation. Trehalose level initially decreased upto 4 hours in all the sets by utilizing pre-synthesized trehalose, thereafter the AdoMet incubated cells showed sharp increase in trehalose content, in 8 hours 3 fold, in 24 hours nearly 5 fold with respect to others. At the point of 48 hours, cells reached stationary phase in all sets and trehalose level was found to increase.

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Basistha, Bipasha, Anil Kumar Ghosh, and Sumita Ghosh. "Regulation of trehalose metabolism by protein methylation in a mutant strain of Saccharomyces cerevisiae." NBU Journal of Plant Sciences 4, no. 1 (2010): 39–45. http://dx.doi.org/10.55734/nbujps.2010.v04i01.007.

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Trechaloseis a non reducing disaccharide occurring in a wide range of organisms, from bacteria, yeast, to lower and higher plants and insects. It is economically important as a potent stress protectant, protein and biological membrane stabilizer: hence biosynthesis of trchalose is an extremely important event. Regulation of trehalose metabolism by protein methylation has been reported from previous works of this laboratory. Trehalose metabolism was monitored during different stages of growth of Saccharomyces cerevisiae. HPLC and enzymatic determination of trehalose. glucose, trehalose 6 phosphate phosphatase TPP) and trehalose 6 phosphate synthase (TPS) were carried out. It was noticed that trchalose, glucose TPP and TPS pcaked at Aso20 during growth but during this period the hydrolyzing enzymes, acid trehalase (AT) and neutral trehalase (NT) are found to be low. Effect of a potent universal methyl group donor S-adenosyl-L-methionine (AdoMet), and a methylation inhibitor, oxidized adenosine (Adox) on trehalose metabolism has been studied. Trehalose metabolism is altered when YPD grown cells were incubated for I hr in presence of cither 1 mM Adox or AdoMet at 30'C and pH 6.0 TPS showed a slight increase in specific activity in cells incubated with AdoMet over Adox. Trehalose level of Adox treated cells were seen to be lower than control throughout the period of incubation. Trehalose level initially decreased upto 4 hours in all the sets by utilizing pre-synthesized trehalose, thereafter the AdoMet incubated cells showed sharp increase in trehalose content, in 8 hours 3 fold, in 24 hours nearly 5 fold with respect to others. At the point of 48 hours, cells reached stationary phase in all sets and trehalose level was found to increase.

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37

Shao, Zuo-min, Jian-hao Ding, De-lei Jiang, Zhi-xiang Liu, Yi-jiangcheng Li, Jiao Wang, Jun Wang, Sheng Sheng, and Fu-an Wu. "Characterization and Functional Analysis of trehalase Related to Chitin Metabolism in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)." Insects 12, no. 4 (April 20, 2021): 370. http://dx.doi.org/10.3390/insects12040370.

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Glyphodes pyloalis Walker (G. pyloalis) is a serious pest on mulberry. Due to the increasing pesticide resistance, the development of new and effective environmental methods to control G. pyloalis is needed. Trehalase is an essential enzyme in trehalose hydrolysis and energy supply, and it has been considered a promising target for insect pest control. However, the specific function of trehalase in G. pyloalis has not been reported. In this study, two trehalase genes (GpTre1 and GpTre2) were identified from our previous transcriptome database. The functions of the trehalase in chitin metabolism were studied by injecting larvae with dsRNAs and trehalase inhibitor, Validamycin A. The open reading frames (ORFs) of GpTre1 and GpTre2 were 1,704 bp and 1,869 bp, which encoded 567 and 622 amino acid residues, respectively. Both of GpTre1 and GpTre2 were mainly expressed in the head and midgut. The highest expression levels of them were in 5th instar during different development stages. Moreover, knockdown both of GpTre1 and GpTre2 by the dsRNAs led to significantly decreased expression of chitin metabolism pathway-related genes, including GpCHSA, GpCDA1, GpCDA2, GpCHT3a, GpCHT7, GpCHSB, GpCHT-h, GpCHT3b, GpPAGM, and GpUAP, and abnormal phenotypes. Furthermore, the trehalase inhibitor, Validamycin A, treatment increased the expressions of GpTre1 and GpTre2, increased content of trehalose, and decreased the levels of glycogen and glucose. Additionally, the inhibitor caused a significantly increased cumulative mortality of G. pyloalis larvae on the 2nd (16%) to 6th (41.3%) day, and decreased the rate of cumulative pupation (72.3%) compared with the control group (95.6%). After the activities of trehalase were suppressed, the expressions of 6 integument chitin metabolism-related genes decreased significantly at 24 h and increased at 48 h. The expressions of GpCHSB and GpCHT-h, involved in chitin metabolism pathway of peritrophic membrane in the midgut, increased at 24 h and 48 h, and there were no changes to GpCHT3b and GpPAGM. These results reveal that GpTre1 and GpTre2 play an essential role in the growth of G. pyloalis by affecting chitin metabolism, and this provides useful information for insect pest control in the future.

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THEVELEIN, J. M., and M. BEULLENS. "Cyclic AMP and the Stimulation of Trehalase Activity in the Yeast Saccharomyces cerevisiae by Carbon Sources, Nitrogen Sources and Inhibitors of Protein Synthesis." Microbiology 131, no. 12 (December 1, 1985): 3199–209. http://dx.doi.org/10.1099/00221287-131-12-3199.

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Conway, Michael J., Douglas P. Haslitt, and Benjamin M. Swarts. "Targeting Aedes aegypti Metabolism with Next-Generation Insecticides." Viruses 15, no. 2 (February 8, 2023): 469. http://dx.doi.org/10.3390/v15020469.

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Aedes aegypti is the primary vector of dengue virus (DENV), zika virus (ZIKV), and other emerging infectious diseases of concern. A key disease mitigation strategy is vector control, which relies heavily on the use of insecticides. The development of insecticide resistance poses a major threat to public health worldwide. Unfortunately, there is a limited number of chemical compounds available for vector control, and these chemicals can have off-target effects that harm invertebrate and vertebrate species. Fundamental basic science research is needed to identify novel molecular targets that can be exploited for vector control. Next-generation insecticides will have unique mechanisms of action that can be used in combination to limit selection of insecticide resistance. Further, molecular targets will be species-specific and limit off-target effects. Studies have shown that mosquitoes rely on key nutrients during multiple life cycle stages. Targeting metabolic pathways is a promising direction that can deprive mosquitoes of nutrition and interfere with development. Metabolic pathways are also important for the virus life cycle. Here, we review studies that reveal the importance of dietary and stored nutrients during mosquito development and infection and suggest strategies to identify next-generation insecticides with a focus on trehalase inhibitors.

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40

Plabutong, Napasawan, Supanuch Ekronarongchai, Nattarika Niwetbowornchai, Steven W. Edwards, Sita Virakul, Direkrit Chiewchengchol, and Arsa Thammahong. "The Inhibitory Effect of Validamycin A on Aspergillus flavus." International Journal of Microbiology 2020 (June 27, 2020): 1–12. http://dx.doi.org/10.1155/2020/3972415.

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Aspergillus flavus is one of the most common isolates from patients with fungal infections. Aspergillus infection is usually treated with antifungal agents, but side effects of these agents are common. Trehalase is an essential enzyme involved in fungal metabolism, and the trehalase inhibitor, validamycin A, has been used to prevent fungal infections in agricultural products. In this study, we observed that validamycin A significantly increased trehalose levels in A. flavus conidia and delayed germination, including decreased fungal adherence. In addition, validamycin A and amphotericin B showed a combinatorial effect on A. flavus ATCC204304 and clinical isolates with high minimum inhibitory concentrations (MICs) of amphotericin B using checkerboard assays. We observed that validamycin A and amphotericin B had a synergistic effect on A. flavus strains resistant to amphotericin B. The MICs in the combination of validamycin A and amphotericin B were at 0.125 μg/mL and 2 μg/mL, respectively. The FICI of validamycin A and amphotericin B of these clinical isolates was about 0.25–0.28 with synergistic effects. No drug cytotoxicity was observed in human bronchial epithelial cells treated with validamycin A using LDH-cytotoxicity assays. In conclusion, this study demonstrated that validamycin A inhibited the growth of A. flavus and delayed conidial germination. Furthermore, the combined effect of validamycin A with amphotericin B increased A. flavus killing, without significant cytotoxicity to human bronchial epithelial cells. We propose that validamycin A could potentially be used in vivo as an alternative treatment for A. flavus infections.

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Wu, Zhiyuan, Yongjie Zhang, Yuyuan Liu, Xuemei Chen, Zhiwen Huang, Xiaoming Zhao, Hongyun He, and Yihao Deng. "Melibiose Confers a Neuroprotection against Cerebral Ischemia/Reperfusion Injury by Ameliorating Autophagy Flux via Facilitation of TFEB Nuclear Translocation in Neurons." Life 11, no. 9 (September 10, 2021): 948. http://dx.doi.org/10.3390/life11090948.

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Autophagic/lysosomal dysfunction is a critical pathogenesis of neuronal injury after ischemic stroke. Trehalose has been validated to restore the impaired autophagy flux by boosting transcription factor EB (TFEB) nuclear translocation, but orally administrated trehalose can be greatly digested by intestinal trehalase before entering into brain. Melibiose (MEL), an analogue of trehalose, may thoroughly exert its pharmacological effects through oral administration due to absence of intestinal melibiase. The present study was to investigate whether melibiose could also confer a neuroprotection by the similar pharmacological mechanism as trehalose did after ischemic stroke. The rats were pretreated with melibiose for 7 days before middle cerebral artery occlusion (MCAO) surgery. Twenty-four hours following MCAO/reperfusion, the cytoplasmic and nuclear TFEB, and the proteins in autophagic/lysosomal pathway at the penumbra were detected by western blot and immunofluorescence, respectively. Meanwhile, the neurological deficit, neuron survival, and infarct volume were assessed to evaluate the therapeutic outcomes. The results showed that the neurological injury was significantly mitigated in MCAO+MEL group, compared with that in MCAO group. Meanwhile, nuclear TFEB expression in neurons at the penumbra was significantly promoted by melibiose. Moreover, melibiose treatment markedly enhanced autophagy flux, as reflected by the reinforced lysosomal capacity and reduced autophagic substrates. Furthermore, the melibiose-elicited neuroprotection was prominently counteracted by lysosomal inhibitor Bafilomycin A1 (Baf-A1). Contrarily, reinforcement of lysosomal capacity with EN6 further improved the neurological performance upon melibiose treatment. Our data suggests that melibiose-augmented neuroprotection may be achieved by ameliorating autophagy flux via facilitation of TFEB nuclear translocation in neurons after ischemic stroke.

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Ogawa, Seiichiro, Koji Sato, and Yasunobu Miyamoto. "Synthesis and trehalase-inhibitory activity of an imino-linked dicarba-α,α-trehalose and analogues thereof." J. Chem. Soc., Perkin Trans. 1, no. 6 (1993): 691–96. http://dx.doi.org/10.1039/p19930000691.

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43

Uchida, Chikara, Tatsuya Yamagishi, Hideo Kitahashi, Yoko Iwaisaki, and Seiichiro Ogawa. "Further chemical modification of trehalase inhibitor trehazolin: Structure and inhibitory-activity relationship of the inhibitor." Bioorganic & Medicinal Chemistry 3, no. 12 (December 1995): 1605–24. http://dx.doi.org/10.1016/0968-0896(95)00147-6.

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44

Kono, Y., M. Takahashi, K. Matsushita, and M. Nishina. "Trehalose synthesis in the fat body of Periplaneta americana and effect of a trehalase inhibitor on it." Medical Entomology and Zoology 48, no. 2 (1997): 164. http://dx.doi.org/10.7601/mez.48.164_2.

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45

GLASHEEN, J. S., and STEVEN C. HAND. "Anhydrobiosis in Embryos of the Brine Shrimp Artemia: Characterization of Metabolic Arrest During Reductions in Cell-Associated Water." Journal of Experimental Biology 135, no. 1 (March 1, 1988): 363–80. http://dx.doi.org/10.1242/jeb.135.1.363.

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Upon entry into the state of anhydrobiosis, trehalose-based energy metabolism is arrested in Artemia embryos (cysts). We have compared changes in the levels of trehalose, glycogen, some glycolytic intermediates and adenylate nucleotides in hydrated embryos observed under conditions of aerobic development with those occurring after transfer to 50moll−1 NaCl. This treatment is known to reduce cellassociated water into a range previously referred to as the ametabolic domain. The trehalose utilization and glycogen synthesis that occur during development of fully hydrated cysts are both blocked during desiccation. Upon return to 0.25 moll−1 NaCl both processes are resumed. Analysis of glycolytic intermediates suggests that the inhibition is localized at the trehalase, hexokinase and phosphofructokinase reactions. ATP level remains constant during the 6-h period of dehydration, as does the adenylate energy charge. An additional dehydration experiment was performed in 5.0moll−1 NaCl containing 50mmoll−1 ammonium chloride (pH9-0). The resulting level of gaseous ammonia in the medium has been shown to maintain an alkaline intracellular pH (pHi) in the embryos. The metabolic response to dehydration under these conditions was very similar to the previous dehydration series. Thus, these results are taken as strong evidence that the metabolic suppression observed during dehydration does not require cellular acidification, in contrast to the pronounced inhibitory role of low pHi during entry of hydrated embryos into the quiescent state of anaerobic dormancy. The arrest of carbohydrate metabolism seen during anhydrobiosis indeed appears to be a strict function of embryo water content.

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NIDETZKY, Bernd, and Christian EIS. "α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors." Biochemical Journal 360, no. 3 (December 10, 2001): 727–36. http://dx.doi.org/10.1042/bj3600727.

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Fungal trehalose phosphorylase is classified as a family 4 glucosyltransferase that catalyses the reversible phosphorolysis of α,α-trehalose with net retention of anomeric configuration. Glucosyl transfer to and from phosphate takes place by the partly rate-limiting interconversion of ternary enzyme–substrate complexes formed from binary enzyme–phosphate and enzyme–α-d-glucopyranosyl phosphate adducts respectively. To advance a model of the chemical mechanism of trehalose phosphorylase, we performed a steady-state kinetic study with the purified enzyme from the basidiomycete fungus Schizophyllum commune by using alternative substrates, inhibitors and combinations thereof in pairs as specific probes of substrate-binding recognition and transition-state structure. Orthovanadate is a competitive inhibitor against phosphate and α-d-glucopyranosyl phosphate, and binds 3×104-fold tighter (Ki≈ 1μM) than phosphate. Structural alterations of d-glucose at C-2 and O-5 are tolerated by the enzyme at subsite +1. They lead to parallel effects of approximately the same magnitude (slope = 1.14; r2 = 0.98) on the reciprocal catalytic efficiency for reverse glucosyl transfer [log (Km/kcat)] and the apparent affinity of orthovanadate determined in the presence of the respective glucosyl acceptor (log Ki). An adduct of orthovanadate and the nucleophile/leaving group bound at subsite +1 is therefore the true inhibitor and displays partial transition state analogy. Isofagomine binds to subsite −1 in the enzyme–phosphate complex with a dissociation constant of 56μM and inhibits trehalose phosphorylase at least 20-fold better than 1-deoxynojirimycin. The specificity of the reversible azasugars inhibitors would be explained if a positive charge developed on C-1 rather than O-5 in the proposed glucosyl cation-like transition state of the reaction. The results are discussed in the context of α-retaining glucosyltransferase mechanisms that occur with and without a β-glucosyl enzyme intermediate.

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47

ANDO, OSAMU, HITOMI SATAKE, KAZUKO ITOI, AKIRA SATO, MUTSUO NAKAJIMA, SHUJI TAKAHASHI, HIDEYUKI HARUYAMA, YOSHIKO OHKUMA, TAKESHI KINOSHITA, and RYUZO ENOKITA. "Trehazolin, a new trehalase inhibitor." Journal of Antibiotics 44, no. 10 (1991): 1165–68. http://dx.doi.org/10.7164/antibiotics.44.1165.

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48

Lee, Do Hee, and Alfred L. Goldberg. "Proteasome Inhibitors Cause Induction of Heat Shock Proteins and Trehalose, Which Together Confer Thermotolerance inSaccharomyces cerevisiae." Molecular and Cellular Biology 18, no. 1 (January 1, 1998): 30–38. http://dx.doi.org/10.1128/mcb.18.1.30.

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ABSTRACT An accumulation in cells of unfolded proteins is believed to be the common signal triggering the induction of heat shock proteins (hsps). Accordingly, in Saccharomyces cerevisiae, inhibition of protein breakdown at 30°C with the proteasome inhibitor MG132 caused a coordinate induction of many heat shock proteins within 1 to 2 h. Concomitantly, MG132, at concentrations that had little or no effect on growth rate, caused a dramatic increase in the cells’ resistance to very high temperature. The magnitude of this effect depended on the extent and duration of the inhibition of proteolysis. A similar induction of hsps and thermotolerance was seen with another proteasome inhibitor, clasto-lactacystin β-lactone, but not with an inhibitor of vacuolar proteases. Surprisingly, when the reversible inhibitor MG132 was removed, thermotolerance decreased rapidly, while synthesis of hsps continued to increase. In addition, exposure to MG132 and 37°C together had synergistic effects in promoting thermotolerance but did not increase hsp expression beyond that seen with either stimulus alone. Although thermotolerance did not correlate with hsp content, another thermoprotectant trehalose accumulated upon exposure of cells to MG132, and the cellular content of this disaccharide, unlike that of hsps, quickly decreased upon removal of MG132. Also, MG132 and 37°C had additive effects in causing trehalose accumulation. Thus, the resistance to heat induced by proteasome inhibitors is not just due to induction of hsps but also requires a short-lived metabolite, probably trehalose, which accumulates when proteolysis is reduced.

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49

OGAWA, S., K. SATO, and Y. MIYAMOTO. "ChemInform Abstract: Synthesis and Trehalase Inhibitory Activity of an Imino-Linked Dicarba- α,α-trehalose and Analogues Thereof." ChemInform 24, no. 33 (August 20, 2010): no. http://dx.doi.org/10.1002/chin.199333257.

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50

Sode, Koji, Eri Akaike, Hiroto Sugiura, and Wakako Tsugawa. "Enzymatic synthesis of a novel trehalose derivative, 3,3′-diketotrehalose, and its potential application as the trehalase enzyme inhibitor." FEBS Letters 489, no. 1 (January 26, 2001): 42–45. http://dx.doi.org/10.1016/s0014-5793(00)02427-3.

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