Drosophila, Chitin and Insect Pest Management

Author(s): Yiwen Wang, Lujuan Gao, Bernard Moussian*

Journal Name: Current Pharmaceutical Design

Volume 26 , Issue 29 , 2020

Become EABM
Become Reviewer
Call for Editor


Insects are a great menace in agriculture and vectors of human diseases. Hence, controlling insect populations is an important issue worldwide. A common strategy to control insects is the application of insecticides. However, insecticides entail three major problems. First, insecticides are chemicals that stress ecosystems and may even be harmful to humans. Second, insecticides are often unspecific and also eradicate beneficial insect species like the honeybee. Third, insects are able to develop resistance to insecticides. Therefore, the efficient generation of new potent insecticides and their intelligent delivery are the major tasks in agriculture. In addition, acceptance or refusal in society is a major issue that has to be considered in the application of a pest management strategy. In this paper, we unify two issues: 1) we illustrate that our molecular knowledge of the chitin synthesis and organization pathways may offer new opportunities to design novel insecticides that are environmentally harmless at the same time being specific to a pest species; and 2) we advocate that the fruit fly Drosophila melanogaster may serve as an excellent model of insect to study the effects of insecticides at the genetic, molecular and histology level in order to better understand their mode of action and to optimize their impact. Especially, chitin synthesis and organization proteins and enzymes are excellently dissected in the fruit fly, providing a rich source for new insecticide targets. Thus, D. melanogaster offers a cheap, efficient and fast assay system to address agricultural questions, as has been demonstrated to be the case in bio-medical research areas.

Keywords: Drosophila melanogaster, insecticide, xenobiotics, chitin, cuticle, bio-medical research.

Carson R. Silent Spring. Foreign affairs (Council on Foreign Relations) 1962; 76: 704.
Junquera P, Hosking B, Gameiro M, Macdonald A. Benzoylphenyl ureas as veterinary antiparasitics. An overview and outlook with emphasis on efficacy, usage and resistance. Parasite 2019; 26: 26.
[http://dx.doi.org/10.1051/parasite/2019026] [PMID: 31041897]
Sun R, Liu C, Zhang H, Wang Q. Benzoylurea Chitin Synthesis Inhibitors. J Agric Food Chem 2015; 63(31): 6847-65.
[http://dx.doi.org/10.1021/acs.jafc.5b02460] [PMID: 26168369]
Abo-Elghar GE, Fujiyoshi P, Matsumura F. Significance of the sulfonylurea receptor (SUR) as the target of diflubenzuron in chitin synthesis inhibition in Drosophila melanogaster and Blattella germanica. Insect Biochem Mol Biol 2004; 34(8): 743-52.
[http://dx.doi.org/10.1016/j.ibmb.2004.03.009] [PMID: 15262279]
Jeschke P, Nauen R. Neonicotinoids-from zero to hero in insecticide chemistry. Pest Manag Sci 2008; 64(11): 1084-98.
[http://dx.doi.org/10.1002/ps.1631] [PMID: 18712805]
Liu Z, Williamson MS, Lansdell SJ, Denholm I, Han Z, Millar NS. A nicotinic acetylcholine receptor mutation conferring target-site resistance to imidacloprid in Nilaparvata lugens (brown planthopper). Proc Natl Acad Sci USA 2005; 102(24): 8420-5.
[http://dx.doi.org/10.1073/pnas.0502901102] [PMID: 15937112]
Eng ML, Stutchbury BJM, Morrissey CA. A neonicotinoid insecticide reduces fueling and delays migration in songbirds. Science 2019; 365(6458): 1177-80.
[http://dx.doi.org/10.1126/science.aaw9419] [PMID: 31515394]
Romeis J, Meissle M, Bigler F. Transgenic crops expressing Bacillus thuringiensis toxins and biological control 2006; 24: 63-71.
Tabashnik BE, Brévault T, Carrière Y. Insect resistance to Bt crops: lessons from the first billion acres. Nat Biotechnol 2013; 31(6): 510-21.
[http://dx.doi.org/10.1038/nbt.2597] [PMID: 23752438]
Zhang H, Tian W, Zhao J, et al. Diverse genetic basis of field-evolved resistance to Bt cotton in cotton bollworm from China. Proc Natl Acad Sci USA 2012; 109(26): 10275-80.
[http://dx.doi.org/10.1073/pnas.1200156109] [PMID: 22689968]
Denholm I, Devine GJ, Williamson MS. Evolutionary genetics. Insecticide resistance on the move. Science 2002; 297(5590): 2222-3.
[http://dx.doi.org/10.1126/science.1077266] [PMID: 12351778]
Louwaars NP. Plant breeding and diversity: A troubled relationship? Euphytica 2018; 214(7): 114.
[http://dx.doi.org/10.1007/s10681-018-2192-5] [PMID: 30996394]
Carpenter JE. Impact of GM crops on biodiversity. GM Crops 2011; 2(1): 7-23.
[http://dx.doi.org/10.4161/gmcr.2.1.15086] [PMID: 21844695]
Sun J. Genetically Modified Foods in China: Regulation, Deregulation, or Governance?. Innovation, Economic Development, and Intellectual Property in India and China - Comparing Six Economic Sectors. Springer Nature 2019; pp. 347-66.
Tagliabue G. The EU legislation on “GMOs” between nonsense and protectionism: An ongoing Schumpeterian chain of public choices. GM Crops Food 2017; 8(1): 57-73.
[http://dx.doi.org/10.1080/21645698.2016.1270488] [PMID: 28001470]
Hundleby PAC, Harwood WA. Impacts of the EU GMO regulatory framework for plant genome editing. Food Energy Secur 2019; 8(2) e00161
[http://dx.doi.org/10.1002/fes3.161] [PMID: 31423300]
Stokstad E. United States relaxes rules for biotech crops. Sciencemagorg 2020.Available at:. https://www.sciencemag.org/news/2020/05/united-states-relaxes-rules-biotech-crops
Denholm, and I EVOLUTIONARY GENETICS: Insecticide Resistance on the Move. Science 2002; 297: 2222-3.
Moussian B. Recent advances in understanding mechanisms of insect cuticle differentiation. Insect Biochem Mol Biol 2010; 40(5): 363-75.
[http://dx.doi.org/10.1016/j.ibmb.2010.03.003] [PMID: 20347980]
Noh MY, Muthukrishnan S, Kramer KJ, Arakane Y. Cuticle formation and pigmentation in beetles. Curr Opin Insect Sci 2016; 17: 1-9.
[http://dx.doi.org/10.1016/j.cois.2016.05.004] [PMID: 27720067]
Liu X, Cooper AMW, Yu Z, Silver K, Zhang J, Zhu KY. Progress and prospects of arthropod chitin pathways and structures as targets for pest management. Pestic Biochem Physiol 2019; 161: 33-46.
[http://dx.doi.org/10.1016/j.pestbp.2019.08.002] [PMID: 31685194]
Zhu KY, Merzendorfer H, Zhang W, Zhang J, Muthukrishnan S. Biosynthesis, Turnover, and Functions of Chitin in Insects. Annu Rev Entomol 2016; 61: 177-96.
[http://dx.doi.org/10.1146/annurev-ento-010715-023933] [PMID: 26982439]
Moussian B, Schwarz H, Bartoszewski S, Nüsslein-Volhard C. Involvement of chitin in exoskeleton morphogenesis in Drosophila melanogaster. J Morphol 2005a; 264(1): 117-30.
[http://dx.doi.org/10.1002/jmor.10324] [PMID: 15747378]
Tonning A, Hemphala J, Tang E, Nannmark U, Samakovlis C, Uv A. A Transient Luminal Chitinous Matrix Is Required to Model Epithelial Tube Diameter in the Drosophila Trachea 2005; 9: 423-30.
Wang Y, Zuber R, Oehl K, Norum M, Moussian B. Report on Drosophila melanogaster larvae without functional tracheae. J Zool (Lond) 2015; 296: 139-45.
Arakane Y, Specht CA, Kramer KJ, Muthukrishnan S, Beeman RW. Chitin synthases are required for survival, fecundity and egg hatch in the red flour beetle, Tribolium castaneum. Insect Biochem Mol Biol 2008; 38(10): 959-62.
[http://dx.doi.org/10.1016/j.ibmb.2008.07.006] [PMID: 18718535]
Moussian B. The apical plasma membrane of chitin-synthesizing epithelia. Insect Sci 2013; 20(2): 139-46.
[http://dx.doi.org/10.1111/j.1744-7917.2012.01549.x] [PMID: 23955854]
Uv A, Moussian B. The apical plasma membrane of Drosophila embryonic epithelia 2010; 89: 208-11.
Locke M. Surface membranes, Golgi complexes, and vacuolar systems. Annu Rev Entomol 2003; 48: 1-27.
[http://dx.doi.org/10.1146/annurev.ento.48.091801.112543] [PMID: 12194907]
Merzendorfer H. The cellular basis of chitin synthesis in fungi and insects: common principles and differences. Eur J Cell Biol 2011; 90(9): 759-69.
[http://dx.doi.org/10.1016/j.ejcb.2011.04.014] [PMID: 21700357]
Merzendorfer H. Insect chitin synthases: a review. J Comp Physiol B 2006; 176(1): 1-15.
[http://dx.doi.org/10.1007/s00360-005-0005-3] [PMID: 16075270]
Van Leeuwen T, Demaeght P, Osborne EJ, et al. Population bulk segregant mapping uncovers resistance mutations and the mode of action of a chitin synthesis inhibitor in arthropods. Proc Natl Acad Sci USA 2012; 109(12): 4407-12.
[http://dx.doi.org/10.1073/pnas.1200068109] [PMID: 22393009]
Mackay TF, Richards S, Stone EA, et al. The Drosophila melanogaster Genetic Reference Panel. Nature 2012; 482(7384): 173-8.
[http://dx.doi.org/10.1038/nature10811] [PMID: 22318601]
Gangishetti U, Veerkamp J, Bezdan D, Schwarz H, Lohmann I, Moussian B. The transcription factor Grainy head and the steroid hormone ecdysone cooperate during differentiation of the skin of Drosophila melanogaster 2012; 21: 283-95.
Luschnig S, Bätz T, Armbruster K, Krasnow MA. serpentine and vermiform encode matrix proteins with chitin binding and deacetylation domains that limit tracheal tube length in Drosophila. Curr Biol 2006; 16(2): 186-94.
[http://dx.doi.org/10.1016/j.cub.2005.11.072] [PMID: 16431371]
Moussian B, Letizia A, Martínez-Corrales G, Rotstein B, Casali A, Llimargas M. Deciphering the genetic programme triggering timely and spatially-regulated chitin deposition. PLoS Genet 2015; 11(1) e1004939
[http://dx.doi.org/10.1371/journal.pgen.1004939] [PMID: 25617778]
Tajiri R, Ogawa N, Fujiwara H, Kojima T. Mechanical Control of Whole Body Shape by a Single Cuticular Protein Obstructor-E in Drosophila melanogaster. PLoS Genet 2017; 13(1) e1006548
[http://dx.doi.org/10.1371/journal.pgen.1006548] [PMID: 28076349]
Pesch YY, Riedel D, Behr M. Drosophila Chitinase 2 is expressed in chitin producing organs for cuticle formation. Arthropod Struct Dev 2017; 46(1): 4-12.
[http://dx.doi.org/10.1016/j.asd.2016.11.002] [PMID: 27832982]
Pesch YY, Riedel D, Behr M. Obstructor A organizes matrix assembly at the apical cell surface to promote enzymatic cuticle maturation in Drosophila. J Biol Chem 2015; 290(16): 10071-82.
[http://dx.doi.org/10.1074/jbc.M114.614933] [PMID: 25737451]
Zuber R, Shaik KS, Meyer F, et al. The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila. Sci Rep 2019; 9(1): 5374.
[http://dx.doi.org/10.1038/s41598-019-41734-9] [PMID: 30926832]
Moussian B, Söding J, Schwarz H, Nüsslein-Volhard C. Retroactive, a membrane-anchored extracellular protein related to vertebrate snake neurotoxin-like proteins, is required for cuticle organization in the larva of Drosophila melanogaster. Dev Dyn 2005; 233(3): 1056-63.
[http://dx.doi.org/10.1002/dvdy.20389] [PMID: 15844167]
Moussian B, Tång E, Tonning A, et al. Drosophila Knickkopf and Retroactive are needed for epithelial tube growth and cuticle differentiation through their specific requirement for chitin filament organization. Development 2006; 133(1): 163-71.
[http://dx.doi.org/10.1242/dev.02177] [PMID: 16339194]
Chaudhari SS, Arakane Y, Specht CA, et al. Knickkopf protein protects and organizes chitin in the newly synthesized insect exoskeleton. Proc Natl Acad Sci USA 2011; 108(41): 17028-33.
[http://dx.doi.org/10.1073/pnas.1112288108] [PMID: 21930896]
Chaudhari SS, Arakane Y, Specht CA, et al. Retroactive maintains cuticle integrity by promoting the trafficking of Knickkopf into the procuticle of Tribolium castaneum. PLoS Genet 2013; 9(1) e1003268
[http://dx.doi.org/10.1371/journal.pgen.1003268] [PMID: 23382702]
Shaik KS, Wang Y, Aravind L, Moussian B. The Knickkopf DOMON domain is essential for cuticle differentiation in Drosophila melanogaster. Arch Insect Biochem Physiol 2014; 86(2): 100-6.
[http://dx.doi.org/10.1002/arch.21165] [PMID: 24723222]
Neville AC. Biology of the arthropod cuticle. Berlin, Heidelberg, New York: Springer Verlag 1975.
Noh MY, Muthukrishnan S, Kramer KJ, Arakane Y. Group I chitin deacetylases are essential for higher order organization of chitin fibers in beetle cuticle. J Biol Chem 2018; 293(18): 6985-95.
[http://dx.doi.org/10.1074/jbc.RA117.001454] [PMID: 29567838]
Yu R, Liu W, Li D, et al. Helicoidal Organization of Chitin in the Cuticle of the Migratory Locust Requires the Function of the Chitin Deacetylase2 Enzyme (LmCDA2). J Biol Chem 2016; 291(47): 24352-63.
[http://dx.doi.org/10.1074/jbc.M116.720581] [PMID: 27637332]
Yu RR, Liu WM, Zhao XM, et al. LmCDA1 organizes the cuticle by chitin deacetylation in Locusta migratoria. Insect Mol Biol 2019; 28(3): 301-12.
[http://dx.doi.org/10.1111/imb.12554] [PMID: 30471154]
Willis JH. Structural cuticular proteins from arthropods: annotation, nomenclature, and sequence characteristics in the genomics era. Insect Biochem Mol Biol 2010; 40(3): 189-204.
[http://dx.doi.org/10.1016/j.ibmb.2010.02.001] [PMID: 20171281]
Cornman RS. Molecular evolution of Drosophila cuticular protein genes. PLoS One 2009; 4(12) e8345
[http://dx.doi.org/10.1371/journal.pone.0008345] [PMID: 20019874]
Gangishetti U, Breitenbach S, Zander M, et al. Effects of benzoylphenylurea on chitin synthesis and orientation in the cuticle of the Drosophila larva 2009; 88: 167-80.
Becq F, Hamon Y, Bajetto A, Gola M, Verrier B, Chimini G. ABC1, an ATP binding cassette transporter required for phagocytosis of apoptotic cells, generates a regulated anion flux after expression in Xenopus laevis oocytes. J Biol Chem 1997; 272(5): 2695-9.
[http://dx.doi.org/10.1074/jbc.272.5.2695] [PMID: 9006906]
Nasonkin I, Alikasifoglu A, Ambrose C, et al. A novel sulfonylurea receptor family member expressed in the embryonic Drosophila dorsal vessel and tracheal system. J Biol Chem 1999; 274(41): 29420-5.
[http://dx.doi.org/10.1074/jbc.274.41.29420] [PMID: 10506204]
Meyer F, Flötenmeyer M, Moussian B. The sulfonylurea receptor Sur is dispensable for chitin synthesis in Drosophila melanogaster embryos. Pest Manag Sci 2013; 69(10): 1136-40.
[http://dx.doi.org/10.1002/ps.3476] [PMID: 23441090]
Douris V, Steinbach D, Panteleri R, et al. Resistance mutation conserved between insects and mites unravels the benzoylurea insecticide mode of action on chitin biosynthesis. Proc Natl Acad Sci USA 2016; 113(51): 14692-7.
[http://dx.doi.org/10.1073/pnas.1618258113] [PMID: 27930336]
UNEP. Global honey bee colony disorders and other threats to insect pollinators 2010.Available at:. http://wedocs.unep.org/handle/20.500.11822/8544
Millar NS, Denholm I. Nicotinic acetylcholine receptors: targets for commercially important insecticides. Invert Neurosci 2007; 7(1): 53-66.
[http://dx.doi.org/10.1007/s10158-006-0040-0] [PMID: 17216290]
Perry T, Heckel DG, McKenzie JA, Batterham P. Mutations in Dalpha1 or Dbeta2 nicotinic acetylcholine receptor subunits can confer resistance to neonicotinoids in Drosophila melanogaster. Insect Biochem Mol Biol 2008; 38(5): 520-8.
[http://dx.doi.org/10.1016/j.ibmb.2007.12.007] [PMID: 18405830]
Chmiel JA, Daisley BA, Burton JP, Reid G. Deleterious Effects of Neonicotinoid Pesticides on Drosophila melanogaster Immune Pathways. MBio 2019; 10(5): 10.
[http://dx.doi.org/10.1128/mBio.01395-19] [PMID: 31575764]
Daisley BA, Trinder M, McDowell TW, et al. Neonicotinoid-induced pathogen susceptibility is mitigated by Lactobacillus plantarum immune stimulation in a Drosophila melanogaster model. Sci Rep 2017; 7(1): 2703.
[http://dx.doi.org/10.1038/s41598-017-02806-w] [PMID: 28578396]
Bravo A, Likitvivatanavong S, Gill SS, Soberón M. Bacillus thuringiensis: A story of a successful bioinsecticide. Insect Biochem Mol Biol 2011; 41(7): 423-31.
[http://dx.doi.org/10.1016/j.ibmb.2011.02.006] [PMID: 21376122]
Saadoun I, Al-Momani F, Obeidat M, Meqdam M, Elbetieha A. Assessment of toxic potential of local Jordanian Bacillus thuringiensis strains on Drosophila melanogaster and Culex sp. (Diptera). J Appl Microbiol 2001; 90(6): 866-72.
[http://dx.doi.org/10.1046/j.1365-2672.2001.01315.x] [PMID: 11412316]
Tounsi S, Jaoua S. Characterization of a novel cry2Aa-type gene from Bacillus thuringiensis subsp. kurstaki. Biotechnol Lett 2003; 25(15): 1219-23.
[http://dx.doi.org/10.1023/A:1025016221891] [PMID: 14514070]
Haller S, Romeis J, Meissle M. Effects of purified or plant-produced Cry proteins on Drosophila melanogaster (Diptera: Drosophilidae) larvae. Sci Rep 2017; 7(1): 11172.
[http://dx.doi.org/10.1038/s41598-017-10801-4] [PMID: 28894124]
Stevens T, Song S, Bruning JB, Choo A, Baxter SW. Expressing a moth abcc2 gene in transgenic Drosophila causes susceptibility to Bt Cry1Ac without requiring a cadherin-like protein receptor. Insect Biochem Mol Biol 2017; 80: 61-70.
[http://dx.doi.org/10.1016/j.ibmb.2016.11.008] [PMID: 27914919]
Rath S, Freiedlaender LG, Reuss R. Diflubenzuron. Residue Monograph prepared by the meeting of the Joint FAO/WHO Expert Committee on Food Additives (JECFA). 81st meeting 1-32.
Comission TE. COMMISSION REGULATION (EU) 2019/91 of 18 January 2019 amending Annexes II, III and V to Regulation (EC) No 396/2005 of the European Parliament and of the Council as regards maximum residue levels for buprofezin, diflubenzuron, ethoxysulfuron, ioxynil, molinate, picoxystrobin and tepraloxydim in or on certain products. Off J. Eur Union 2019; 74-85.
Fletcher SJ, Reeves PT, Hoang BT, Mitter N. A Perspective on RNAi-Based Biopesticides. Front Plant Sci 2020; 11: 51.
[http://dx.doi.org/10.3389/fpls.2020.00051] [PMID: 32117388]
Alamalakala L, Parimi S, Patel N, Char B. Insect RNAi: Integrating a New Tool in the Crop Protection Toolkit. Trends in Insect Molecular Biology and Biotechnology 2020; pp. 193-232.
Zhang M, Ji Y, Zhang X, et al. The putative chitin deacetylases Serpentine and Vermiform have non-redundant functions during Drosophila wing development. Insect Biochem Mol Biol 2019; 110: 128-35.
[http://dx.doi.org/10.1016/j.ibmb.2019.05.008] [PMID: 31108167]
Li K, Zhang X, Zuo Y, Liu W, Zhang J, Moussian B. Timed Knickkopf function is essential for wing cuticle formation in Drosophila melanogaster. Insect Biochem Mol Biol 2017; 89: 1-10.
[http://dx.doi.org/10.1016/j.ibmb.2017.08.003] [PMID: 28821399]
Arakane Y, Baguinon MC, Jasrapuria S, et al. Both UDP N-acetylglucosamine pyrophosphorylases of Tribolium castaneum are critical for molting, survival and fecundity. Insect Biochem Mol Biol 2011; 41(1): 42-50.
[http://dx.doi.org/10.1016/j.ibmb.2010.09.011] [PMID: 20920581]
Arakane Y, Muthukrishnan S, Kramer KJ, et al. The Tribolium chitin synthase genes TcCHS1 and TcCHS2 are specialized for synthesis of epidermal cuticle and midgut peritrophic matrix. Insect Mol Biol 2005; 14(5): 453-63.
[http://dx.doi.org/10.1111/j.1365-2583.2005.00576.x] [PMID: 16164601]
Ye C, Jiang YD, An X, et al. Effects of RNAi-based silencing of chitin synthase gene on moulting and fecundity in pea aphids (Acyrthosiphon pisum). Sci Rep 2019; 9(1): 3694.
[http://dx.doi.org/10.1038/s41598-019-39837-4] [PMID: 30842508]
Singh AD, Wong S, Ryan CP, Whyard S. Oral delivery of double-stranded RNA in larvae of the yellow fever mosquito, Aedes aegypti: implications for pest mosquito control. J Insect Sci 2013; 13: 69.
[http://dx.doi.org/10.1673/031.013.6901] [PMID: 24224468]
Mohammed AMA, Diab MR, Abdelsattar M, Khalil SMS. Characterization and RNAi-mediated knockdown of Chitin Synthase A in the potato tuber moth, Phthorimaea operculella. Sci Rep 2017; 7(1): 9502.
[http://dx.doi.org/10.1038/s41598-017-09858-y] [PMID: 28842624]
Shi JF, Mu LL, Chen X, Guo WC, Li GQ. RNA interference of chitin synthase genes inhibits chitin biosynthesis and affects larval performance in Leptinotarsa decemlineata (Say). Int J Biol Sci 2016; 12(11): 1319-31.
[http://dx.doi.org/10.7150/ijbs.14464] [PMID: 27877084]
Macedo LLP, Antonino de Souza JD JunioR, Coelho RR, et al. Knocking down chitin synthase 2 by RNAi is lethal to the cotton boll weevil. Biotechnol Res Innovation 2017; 1: 72-86.
Lopez SBG, Guimarães-Ribeiro V, Rodriguez JVG, et al. RNAi-based bioinsecticide for Aedes mosquito control. Sci Rep 2019; 9(1): 4038.
[http://dx.doi.org/10.1038/s41598-019-39666-5] [PMID: 30858430]
Zhang JD, Sach-Peltason L, Kramer C, Wang K, Ebeling M. Multiscale modelling of drug mechanism and safety. Drug Discov Today 2020; 25(3): 519-34.
[http://dx.doi.org/10.1016/j.drudis.2019.12.009] [PMID: 31899257]
Schneider P, Walters WP, Plowright AT, et al. Rethinking drug design in the artificial intelligence era. Nat Rev Drug Discov 2020; 19(5): 353-64.
[http://dx.doi.org/10.1038/s41573-019-0050-3] [PMID: 31801986]
Malathi K, Ramaiah S. Bioinformatics approaches for new drug discovery: a review. Biotechnol Genet Eng Rev 2018; 34(2): 243-60.
[http://dx.doi.org/10.1080/02648725.2018.1502984] [PMID: 30064294]
Arakane Y, Muthukrishnan S. Insect chitinase and chitinase-like proteins. Cell Mol Life Sci 2010; 67(2): 201-16.
[http://dx.doi.org/10.1007/s00018-009-0161-9] [PMID: 19816755]
Duan Y, Liu T, Zhou Y, Dou T, Yang Q. Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine. J Biol Chem 2018; 293(40): 15429-38.
[http://dx.doi.org/10.1074/jbc.RA118.004351] [PMID: 30135205]
Fan XJ, Yang C, Zhang C, Ren H, Zhang JD. Cloning, Site-Directed Mutagenesis, and Functional Analysis of Active Residues in Lymantria dispar Chitinase. Appl Biochem Biotechnol 2018; 184(1): 12-24.
[http://dx.doi.org/10.1007/s12010-017-2524-2] [PMID: 28577192]
Liu T, Chen L, Zhou Y, Jiang X, Duan Y, Yang Q. Structure, Catalysis, and Inhibition of Chi-h, the Lepidoptera-exclusive Insect Chitinase. J Biol Chem 2017; 292(6): 2080-8.
[http://dx.doi.org/10.1074/jbc.M116.755330] [PMID: 28053084]

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2020
Published on: 03 September, 2020
Page: [3546 - 3553]
Pages: 8
DOI: 10.2174/1381612826666200721002354
Price: $65

Article Metrics

PDF: 31