Papilionidae). Insect Biochem Mol Biol 27:377–385. https://doi.org/10.1016/S0965-1748(97)
00009-X
92. Li X, Baudry J, Berenbaum MR, Schuler MA (2004) Structural and functional divergence of
insect CYP6B proteins: from specialist to generalist cytochrome P450. Proc Natl Acad Sci
101:2939–2944. https://doi.org/10.1073/pnas.0308691101
93. Li X, Berenbaum MR, Schuler MA (2002) Cytochrome P450 and actin genes expressed in
Helicoverpa zea and Helicoverpa armigera: Paralogy/orthology identification, gene conversion and evolution. Insect Biochem Mol Biol 32:311–320. https://doi.org/10.1016/S09651748(01)00092-3
94. Sasabe M, Wen Z, Berenbaum MR, Schuler MA (2004) Molecular analysis of CYP321A1, a
novel cytochrome P450 involved in metabolism of plant allelochemicals (furanocoumarins)
and insecticides (cypermethrin) in Helicoverpa zea. Gene 338:163–175. https://doi.org/
10.1016/j.gene.2004.04.028
95. Li X, Schuler MA, Berenbaum MR (2002) Jasmonate and salicylate induce expression of
herbivore cytochrome P450 genes. Nature 419:712–715. https://doi.org/10.1038/nature01003
96. Calla B, Noble K, Johnson RM (2017) Cytochrome P450 diversification and hostplant
utilization patterns in specialist and generalist moths: birth, death and adaptation. Mol Ecol
26:6021–6035. https://doi.org/10.1111/mec.14348
97. Cabrera-Brandt MA, Fuentes-Contreras E, Figueroa CC (2010) Differences in the detoxification metabolism between two clonal lineages of the aphid Myzus persicae (Sulzer) (Hemiptera:
Aphididae) reared on tobacco (Nicotiana tabacum L.). Chilean J Agric Res 70:567–575.
https://doi.org/10.4067/S0718-58392010000400006
98. Lindroth RL, Weisbrod AV (1991) Genetic variation in response of the gypsy moth to aspen
phenolic glycosides. Biochem Syst Ecol 19:97–103. https://doi.org/10.1016/0305-1978(91)
90031-T
99. Lindroth RL (1989) Host plant alteration of detoxication activity in Papilio glaucus. Entomol
Exp Appl 50(1):29–35. https://doi.org/10.1111/j.1570-7458.1989.tb02310.x
100. Ghumare SS, Mukherjee SN, Sharma RN (1989) Effect of rutin on the neonate sensitivity, dietary utilization and mid-gut carboxylesterase activity of Spodoptera litura
(Fabricius) (Lepidoptera: Noctuidae). Proc Anim Sci 98:399–404. https://doi.org/10.1007/
BF03179652
101. Cai QN, Han Y, Cao YZ (2009) Detoxification of gramine by the cereal aphid sitobion avenae.
J Chem Ecol 35:320–325. https://doi.org/10.1007/s10886-009-9603-y
102. Yu QY, Lu C, Li WL (2009) Annotation and expression of carboxylesterases in
the silkworm, Bombyx mori. BMC Genomics 10:1–14. https://doi.org/10.1186/1471-216410-553
103. Ketterman AJ, Saisawang C, Wongsantichon J (2011) Insect glutathione transferases. Drug
Metab Rev 43:253–265. https://doi.org/10.3109/03602532.2011.552911
104. Pavlidi N, Vontas J, Van Leeuwen T (2018) The role of glutathione S-transferases (GSTs) in
insecticide resistance in crop pests and disease vectors. Curr Opin Insect Sci 27:97–102.
https://doi.org/10.1016/j.cois.2018.04.007
105. Berenbaum MR, Johnson RM (2015) Xenobiotic detoxification pathways in honey bees. Curr
Opin Insect Sci 10:51–58. https://doi.org/10.1016/j.cois.2015.03.005
106. Deponte M (2013) Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochim Biophys Acta 1830:3217–3266. https://doi.org/10.1016/j.
bbagen.2012.09.018
107. Enayati AA, Ranson H, Hemingway J (2005) Insect glutathione transferases and
insecticide resistance. Insect Mol Biol 14:3–8. https://doi.org/10.1111/j.13652583.2004.00529.x
108. Ahn SJ, Vogel H, Heckel DG (2012) Comparative analysis of the UDP-glycosyltransferase
multigene family in insects. Insect Biochem Mol Biol 42:133–147. https://doi.org/10.1016/j.
ibmb.2011.11.006
109. Luque T, Okano K, O’Reilly DR (2002) Characterization of a novel silkworm (Bombyx mori)
phenol UDP-glucosyltransferase. Eur J Biochem 269:819–825. https://doi.org/10.1046/
j.0014-2956.2001.02723.x
2 Plant-Insect Interaction: The Saga of Molecular Coevolution
43
00009-X
92. Li X, Baudry J, Berenbaum MR, Schuler MA (2004) Structural and functional divergence of
insect CYP6B proteins: from specialist to generalist cytochrome P450. Proc Natl Acad Sci
101:2939–2944. https://doi.org/10.1073/pnas.0308691101
93. Li X, Berenbaum MR, Schuler MA (2002) Cytochrome P450 and actin genes expressed in
Helicoverpa zea and Helicoverpa armigera: Paralogy/orthology identification, gene conversion and evolution. Insect Biochem Mol Biol 32:311–320. https://doi.org/10.1016/S09651748(01)00092-3
94. Sasabe M, Wen Z, Berenbaum MR, Schuler MA (2004) Molecular analysis of CYP321A1, a
novel cytochrome P450 involved in metabolism of plant allelochemicals (furanocoumarins)
and insecticides (cypermethrin) in Helicoverpa zea. Gene 338:163–175. https://doi.org/
10.1016/j.gene.2004.04.028
95. Li X, Schuler MA, Berenbaum MR (2002) Jasmonate and salicylate induce expression of
herbivore cytochrome P450 genes. Nature 419:712–715. https://doi.org/10.1038/nature01003
96. Calla B, Noble K, Johnson RM (2017) Cytochrome P450 diversification and hostplant
utilization patterns in specialist and generalist moths: birth, death and adaptation. Mol Ecol
26:6021–6035. https://doi.org/10.1111/mec.14348
97. Cabrera-Brandt MA, Fuentes-Contreras E, Figueroa CC (2010) Differences in the detoxification metabolism between two clonal lineages of the aphid Myzus persicae (Sulzer) (Hemiptera:
Aphididae) reared on tobacco (Nicotiana tabacum L.). Chilean J Agric Res 70:567–575.
https://doi.org/10.4067/S0718-58392010000400006
98. Lindroth RL, Weisbrod AV (1991) Genetic variation in response of the gypsy moth to aspen
phenolic glycosides. Biochem Syst Ecol 19:97–103. https://doi.org/10.1016/0305-1978(91)
90031-T
99. Lindroth RL (1989) Host plant alteration of detoxication activity in Papilio glaucus. Entomol
Exp Appl 50(1):29–35. https://doi.org/10.1111/j.1570-7458.1989.tb02310.x
100. Ghumare SS, Mukherjee SN, Sharma RN (1989) Effect of rutin on the neonate sensitivity, dietary utilization and mid-gut carboxylesterase activity of Spodoptera litura
(Fabricius) (Lepidoptera: Noctuidae). Proc Anim Sci 98:399–404. https://doi.org/10.1007/
BF03179652
101. Cai QN, Han Y, Cao YZ (2009) Detoxification of gramine by the cereal aphid sitobion avenae.
J Chem Ecol 35:320–325. https://doi.org/10.1007/s10886-009-9603-y
102. Yu QY, Lu C, Li WL (2009) Annotation and expression of carboxylesterases in
the silkworm, Bombyx mori. BMC Genomics 10:1–14. https://doi.org/10.1186/1471-216410-553
103. Ketterman AJ, Saisawang C, Wongsantichon J (2011) Insect glutathione transferases. Drug
Metab Rev 43:253–265. https://doi.org/10.3109/03602532.2011.552911
104. Pavlidi N, Vontas J, Van Leeuwen T (2018) The role of glutathione S-transferases (GSTs) in
insecticide resistance in crop pests and disease vectors. Curr Opin Insect Sci 27:97–102.
https://doi.org/10.1016/j.cois.2018.04.007
105. Berenbaum MR, Johnson RM (2015) Xenobiotic detoxification pathways in honey bees. Curr
Opin Insect Sci 10:51–58. https://doi.org/10.1016/j.cois.2015.03.005
106. Deponte M (2013) Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochim Biophys Acta 1830:3217–3266. https://doi.org/10.1016/j.
bbagen.2012.09.018
107. Enayati AA, Ranson H, Hemingway J (2005) Insect glutathione transferases and
insecticide resistance. Insect Mol Biol 14:3–8. https://doi.org/10.1111/j.13652583.2004.00529.x
108. Ahn SJ, Vogel H, Heckel DG (2012) Comparative analysis of the UDP-glycosyltransferase
multigene family in insects. Insect Biochem Mol Biol 42:133–147. https://doi.org/10.1016/j.
ibmb.2011.11.006
109. Luque T, Okano K, O’Reilly DR (2002) Characterization of a novel silkworm (Bombyx mori)
phenol UDP-glucosyltransferase. Eur J Biochem 269:819–825. https://doi.org/10.1046/
j.0014-2956.2001.02723.x
2 Plant-Insect Interaction: The Saga of Molecular Coevolution
43