Genomics-based approaches to screening carboxylesterase-like genes potentially involved in malathion resistance in oriental migratory locust (Locusta migratoria manilensis)

Pest Management Science

Volumn 67, Issue 2, 2011, Pages 183-190

  Zhang, Jianzhen ^a   Zhang, Jianqin ^a   Yang, Meiling ^a   Jia, Qidong ^b   Guo, Yaping ^a   Ma, Enbo ^a   Zhu, Kun Yan ^c  

^a SHANXI UNIVERSITY   (China)

^b NANJING AGRICULTURAL UNIVERSITY   (China)

^c KANSAS STATE UNIVERSITY   (United States)

Author keywords

Carboxylesterase; Expressed sequence tag; Insecticide resistance; Locusta migratoria manilensis; RNA interference

Indexed keywords

CARBOXYLESTERASE; INSECT PROTEIN; INSECTICIDE; MALATHION;

ADULT; BIOASSAY; DATABASE; ENZYME ACTIVITY; GENE EXPRESSION; GENOMICS; LOCUST; MALATHION; MIGRATORY SPECIES; MORTALITY; PESTICIDE RESISTANCE;

ANIMAL; ARTICLE; DRUG EFFECT; ENZYMOLOGY; EXPRESSED SEQUENCE TAG; GENETICS; GENOMICS; INSECTICIDE RESISTANCE; LOCUST; METABOLISM; NUCLEIC ACID DATABASE; PHYSIOLOGY; POPULATION MIGRATION;

ANIMAL MIGRATION; ANIMALS; CARBOXYLESTERASE; DATABASES, NUCLEIC ACID; EXPRESSED SEQUENCE TAGS; GENOMICS; INSECT PROTEINS; INSECTICIDE RESISTANCE; INSECTICIDES; LOCUSTA MIGRATORIA; MALATHION;

LOCUSTA MIGRATORIA MANILENSIS;

EID: 78650988578     PISSN: 1526498X     EISSN: 15264998     Source Type: Journal    
DOI: 10.1002/ps.2049     Document Type: Article

References (34)

1. Chen YL, Main achievement of research and management of migratory locust in China. Entomol Knowl 37: 50-58 (2000).
2. Zhu EL, The Occurrence and Management of Oriental Migratory Locust. Chinese Agricultural Press, Beijing, China (1999).
3. Chen YL, The characteristic, cause and ecological management of locust disaster. Bull Biol 35: 1-5 (2000).
4. Xia JY and Huang H, Analysis on the outbreak of Locusta migratoria manilensis and its control strategies. Plant Protect Tech Ext 22: 7-10 (2002).
5. Ma EB, He YP and Zhu KY, Comparative studies of acetylcholinesterases purified from two field populations of the oriental migratory locust (Locusta migratoria manilensis): implications of insecticide resistance. Pestic Biochem Physiol 78: 67-77 (2004).
6. He YP, Ma EB and Zhu KY, Characterizations of general esterases in relation to malathion susceptibility in two field populations of the oriental migratory locust, Locusta migratoria manilensis (Meyen). Pestic Biochem Physiol 78: 103-113 (2004).
7. Yang ML, Zhang JZ, Zhu KY, Xuan T, Liu XJ, Guo YP, et al., Increased activity and reduced sensitivity of acetylcholinesterase associated with malathion resistance in a field population of the oriental migratory locust, Locusta migratoria manilensis (Meyen). Pestic Biochem Physiol 91: 32-38 (2008).
8. Yang ML, Zhang JZ, Zhu KY, Xuan T, Liu XJ, Guo YP, et al, Mechanisms of organophosphate resistance in a field population of oriental migratory locust, Locusta migratoria manilensis (Meyen). Arch Biochem Physiol 69: 1-10 (2008).
9. Oakeshott JG, Claudianos C, Campbell PM, Newcomb RD and Russell RJ, Biochemical genetics and genomics of insect esterases, in Comprehensive Molecular Insect Science. Vol. 5, ed. by Gilbert LI, Iatrou K and Gill S. Elsevier, Oxford, UK, pp. 309-381 (2005).
10. Strode C, Wondji CS, David JP, Hawkes NJ, Lumjuan N, Nelson DR, et al., Genomic analysis of detoxification genes in the mosquito Aedes aegypti. Insect Biochem Mol Biol 38: 113-123 (2008).
11. Kang L, Chen XY, Zhou Y, Liu BW, Zheng W, Li RQ, et al., The analysis of large-scale gene expression correlated to the phase changes of the migratory locust. Proc Natl Acad Sci USA 101: 17 611-17 615 (2004).
12. Ma ZY, Yu J and Kang L, LocustDB: a relational database for the transcriptome and biology of the migratory locust (Locusta migratoria). BMC Genomics 7: 11 (2006).
13. Satoh T and Hosokawa M, Molecular aspects of carboxylesterase isoforms in comparison with other esterases. Toxicol Let 82-83: 439-445 (1995).
14. Pfaffl MW, A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: 2002-2007 (2001).
15. Zhu KY and Brindley WA, Properties of esterases from Lygus hesperus Knight (Hemiptera: Miridae) and the roles of the esterases in insecticide resistance. J Econ Entomol 83: 725-732 (1990).
16. Zhu KY, Lee SH and Clark JM, A point mutation of acetylcholinesterase associated with azinphosmethyl resistance and reduced fitness in Colorado potato beetle. Pestic Biochem Physiol 55: 100-108 (1996).
17. Zhu KY and Clark JM, Validation of a point mutation of acetylcholinesterase in Colorado potato beetle by polymerase chain reaction coupled to enzyme inhibition assay. Pestic Biochem Physiol 57: 28-35 (1997).
18. Baker JE, Fabrick JA and Zhu KY, Characterization of esterases in malathion-resistant and susceptible strains of the pteromalid parasitoid Anisopteromalus calandrae. Insect Biochem Mol Biol 28: 1039-1050 (1998).
19. Li XC, Schuler MA and Berenbaum MR, Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics. Annu Rev Entomol 52: 231-253 (2007).
20. Devonshire AL and Sawicki RM, Insecticide-resistant Myzus persicae as an example of evolution by gene duplication. Nature 280: 140-141 (1979).
21. Field LM, Devonshire AL and Forde BG, Molecular evidence that insecticide resistance in peach-potato aphid (Myzus persicae Sulz.) results from amplification of an esterase gene. Biochem J 251: 309-312 (1988).
22. Rooker S, Guillemaud T, Bergé J, Pasteur N and Raymond M, Coamplification of esterase A and B genes as a single unit in Culex pipiens mosquitoes. Heredity 77: 555-561 (1996).
23. Raymond M, Chevillon C, Guillemaud T, Lenormand T and Pasteur N, An overview of the evolution of overproduced esterases in the mosquito Culex pipiens. Phil Trans R Soc London B Biol Sci 353: 1707-1711 (1998).
24. Vontas JG, Small GJ and Hemingway J, Comparison of esterase gene amplification, gene expression and esterase activity in insecticide susceptible and resistant strains of the brown planthopper, Nilaparvata lugens (Stål). Insect Mol Biol 9: 655-660 (2000).
25. Small GJ and Hemingway J, Molecular characterization of the amplified carboxylesterase gene associated with organophosphorus insecticide resistance in the brown planthopper, Nilaparvata lugens. Insect Mol Biol 9: 647-653 (2000).
26. Pan YO, Guo HL and Gao XW, Carboxylesterase activity, cDNA sequence, and gene expression in malathion susceptible and resistant strains of the cotton aphid, Aphis gossypii. Comp Biochem Physiol, Part B 152: 266-270 (2009).
27. Alon M, Alon F, Nauen R and Morin S, Organophosphates resistance in the B-biotype of Bemisia tabaci (Hemiptera:Aleyrodidae) is associated with a point mutation in an ace1-type acetylcholinesterase and overexpression of carboxylesterase. Insect Biochem Mol Biol 38: 940-949 (2008).
28. Cui F, Weill M, Berthomieu A, Raymond M and Qiao CL, Characterization of novel esterases in insecticide-resistant mosquitoes. Insect Biochem Mol Biol 37: 1131-1137 (2007).
29. Newcomb RD, Campbell PM, Ollis DL, Cheah E, Russell RJ and Oakeshott JG, A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly. Proc Natl Acad Sci USA 94: 7464-7468 (1997).
30. Oakeshott JG, Devonshire AL, Claudianos C, Sutherland TD, Horne I, Campbell PM, et al., Comparing the organophosphorus and carbamate insecticide resistance mutations in cholin- and carboxyl-esterases. Chem-Biol Interact 157-158: 269-275 (2005).
31. Tittiger C and Walker VK, Isolation and characterization of an unamplified esterase B3 gene from malathion-resistant Culex tarsalis. Biochem Genet 35: 119-138 (1997).
32. Lan WS, Cong J, Jiang H, Jiang SR and Qiao CL, Expression and characterization of carboxylesterase E4 gene from peach-potato aphid (Myzus persicae) for degradation of carbaryl and malathion. Biotechnol Lett 27: 1141-1146 (2005).
33. Akpan BE and Okorie TG, Allometric growth and performance of the gastric caeca of Zonocerus variegatus (L.) (Orthoptera: Pyrgomorphidae). Acta Entomol Sinica 46: 558-566 (2003).
34. Holmes RS, Cox LA and VandeBerg JL, Mammalian carboxylesterase 5: comparative biochemistry and genomics. Comp Biochem Physiol Part D 3: 195-204 (2008).