Detection of Chitin Synthase Mutations in Lufenuron-Resistant in China

Overview

Journal Insects

Specialty Biology

Date 2022 Oct 27

PMID 36292911

Authors

Sheng-Lan Lv

Zheng-Yi Xu

Ming-Jian Li

Amosi Leonard Mbuji

Meng Gu

Lei Zhang

Xi-Wu Gao

Affiliations

Soon will be listed here.

Abstract

(J. E. Smith), is commonly known as fall armyworm, native to tropical and subtropical regions of America, is an important migratory agricultural pest. It is important to understand the resistance and internal mechanism of action of against lufenuron in China. Lufenuron is one of the main insecticides recommended for field use in China and has a broad prospect in the future. We conducted a bioassay using the diet-overlay method and found that the current in China are still at a low level of resistance to lufenuron. Secondly, we examined whether the mutation I1040M (I1042M in Plutella xylostella), associated with lufenuron resistance, was produced in the field. And then we tested the expression of chitin synthase SfCHSA and SfCHSB in different tissues, and the changes of these two genes after lufenuron induction. The results showed that there is still no mutation generation in China and there is a significant change in the expression of SfCHSA under the effect of lufenuron. In conclusion, our study suggests that field populations in 2019 and 2020 were less resistant to lufenuron. In fall armyworm, chitin synthases included SfCHSA and SfCHSB genes, and after induction treatment with lufenuron, the expression of the SfCHSA gene was significantly increased. In SfCHSA, no mutation has been detected in the site associated with lufenuron resistance. Secondly, in larvae, the SfCHSA gene was the highest in the head of the larvae, followed by the integument; while the SfCHSB gene was mainly concentrated in the midgut. Therefore, we believe that the SfCHSA gene plays a greater role in the resistance of to lufenuron than the SfCHSB gene. It is worth noting that understanding the level of resistance to lufenuron in China, the main mechanism of action of lufenuron on larvae, and the mechanism of resistance to lufenuron in will help in crop protection as well as in extending the life span of this insecticide.

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References

Nascimento A, Farias J, Bernardi D, Horikoshi R, Omoto C . Genetic basis of Spodoptera frugiperda (Lepidoptera: Noctuidae) resistance to the chitin synthesis inhibitor lufenuron. Pest Manag Sci. 2015; 72(4):810-5. DOI: 10.1002/ps.4057. View

Wilson T, Cryan J . Lufenuron, a chitin-synthesis inhibitor, interrupts development of Drosophila melanogaster. J Exp Zool. 1997; 278(1):37-44. DOI: 10.1002/(sici)1097-010x(19970501)278:1<37::aid-jez4>3.0.co;2-7. View

Lv S, Shi Y, Zhang J, Liang P, Zhang L, Gao X . Detection of ryanodine receptor target-site mutations in diamide insecticide-resistant Spodoptera frugiperda in China. Insect Sci. 2021; 28(3):639-648. DOI: 10.1111/1744-7917.12896. View

Zhang J, Liu X, Zhang J, Li D, Sun Y, Guo Y . Silencing of two alternative splicing-derived mRNA variants of chitin synthase 1 gene by RNAi is lethal to the oriental migratory locust, Locusta migratoria manilensis (Meyen). Insect Biochem Mol Biol. 2010; 40(11):824-33. DOI: 10.1016/j.ibmb.2010.08.001. View

Tetreau G, Cao X, Chen Y, Muthukrishnan S, Jiang H, Blissard G . Overview of chitin metabolism enzymes in Manduca sexta: Identification, domain organization, phylogenetic analysis and gene expression. Insect Biochem Mol Biol. 2015; 62:114-26. DOI: 10.1016/j.ibmb.2015.01.006. View

Zimoch L, Merzendorfer H . Immunolocalization of chitin synthase in the tobacco hornworm. Cell Tissue Res. 2002; 308(2):287-97. DOI: 10.1007/s00441-002-0546-7. View

Bolognesi R, Arakane Y, Muthukrishnan S, Kramer K, Terra W, Ferreira C . Sequences of cDNAs and expression of genes encoding chitin synthase and chitinase in the midgut of Spodoptera frugiperda. Insect Biochem Mol Biol. 2005; 35(11):1249-59. DOI: 10.1016/j.ibmb.2005.06.006. View

Van Leeuwen T, Demaeght P, Osborne E, Dermauw W, Gohlke S, Nauen R . Population bulk segregant mapping uncovers resistance mutations and the mode of action of a chitin synthesis inhibitor in arthropods. Proc Natl Acad Sci U S A. 2012; 109(12):4407-12. PMC: 3311382. DOI: 10.1073/pnas.1200068109. View

Giraudo M, Hilliou F, Fricaux T, Audant P, Feyereisen R, Goff G . Cytochrome P450s from the fall armyworm (Spodoptera frugiperda): responses to plant allelochemicals and pesticides. Insect Mol Biol. 2014; 24(1):115-28. DOI: 10.1111/imb.12140. View

10.

Merzendorfer H . Insect chitin synthases: a review. J Comp Physiol B. 2005; 176(1):1-15. DOI: 10.1007/s00360-005-0005-3. View

11.

Suzuki Y, Shiotsuki T, Jouraku A, Miura K, Minakuchi C . Benzoylurea resistance in western flower thrips (Thysanoptera: Thripidae): the presence of a point mutation in . J Pestic Sci. 2018; 42(3):93-96. PMC: 6183332. DOI: 10.1584/jpestics.D17-023. View

12.

Merzendorfer H, Zimoch L . Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J Exp Biol. 2003; 206(Pt 24):4393-412. DOI: 10.1242/jeb.00709. View

13.

Zhang J, Zhu K . Characterization of a chitin synthase cDNA and its increased mRNA level associated with decreased chitin synthesis in Anopheles quadrimaculatus exposed to diflubenzuron. Insect Biochem Mol Biol. 2006; 36(9):712-25. DOI: 10.1016/j.ibmb.2006.06.002. View

14.

Zimoch L, Hogenkamp D, Kramer K, Muthukrishnan S, Merzendorfer H . Regulation of chitin synthesis in the larval midgut of Manduca sexta. Insect Biochem Mol Biol. 2005; 35(6):515-27. DOI: 10.1016/j.ibmb.2005.01.008. View

15.

Douris V, Steinbach D, Panteleri R, Livadaras I, Pickett J, Van Leeuwen T . Resistance mutation conserved between insects and mites unravels the benzoylurea insecticide mode of action on chitin biosynthesis. Proc Natl Acad Sci U S A. 2016; 113(51):14692-14697. PMC: 5187681. DOI: 10.1073/pnas.1618258113. View

16.

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. DOI: 10.1016/j.ejcb.2011.04.014. View

17.

Wang Y, Fan H, Huang H, Xue J, Wu W, Bao Y . Chitin synthase 1 gene and its two alternative splicing variants from two sap-sucking insects, Nilaparvata lugens and Laodelphax striatellus (Hemiptera: Delphacidae). Insect Biochem Mol Biol. 2012; 42(9):637-46. DOI: 10.1016/j.ibmb.2012.04.009. View

18.

Boaventura D, Bolzan A, Padovez F, Okuma D, Omoto C, Nauen R . Detection of a ryanodine receptor target-site mutation in diamide insecticide resistant fall armyworm, Spodoptera frugiperda. Pest Manag Sci. 2019; 76(1):47-54. DOI: 10.1002/ps.5505. View

19.

Bolzan A, Padovez F, Nascimento A, Kaiser I, Lira E, Amaral F . Selection and characterization of the inheritance of resistance of Spodoptera frugiperda (Lepidoptera: Noctuidae) to chlorantraniliprole and cross-resistance to other diamide insecticides. Pest Manag Sci. 2019; 75(10):2682-2689. DOI: 10.1002/ps.5376. View

20.

Arakane Y, Hogenkamp D, Zhu Y, Kramer K, Specht C, Beeman R . Characterization of two chitin synthase genes of the red flour beetle, Tribolium castaneum, and alternate exon usage in one of the genes during development. Insect Biochem Mol Biol. 2004; 34(3):291-304. DOI: 10.1016/j.ibmb.2003.11.004. View