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Journal of Chemical Ecology

, Volume 15, Issue 7, pp 2019–2029 | Cite as

Chemical ecology of the luna moth

Effects of host plant on detoxification enzyme activity
  • Richard L. Lindroth
Article

Abstract

The effects of food plant on larval performance and midgut detoxification enzymes were investigated in larvae of the luna moth,Actias luna. Neonate larvae were fed leaves of black cherry, cottonwood, quaking aspen, white willow, red oak, white oak, tulip tree, paper birch, black walnut, butternut, or shagbark hickory. First instar survival, larval duration, and pupal weights were monitored as indices of food quality. Midgut enzyme preparations from fifth instars were assayed for β-glucosidase, quinone reductase, polysubstrate monooxygenase, esterase, and glutathione transferase activities. Larval survival on seven of the 11 plant species, including several recorded host plants, was extremely poor. Larvae performed well, and quite similarly, on birch, walnut, butternut, and hickory. Activities of all enzyme systems except β-glucosidase were significantly influenced by larval host plant. Of the systems assayed, quinone reductase and glutathione transferase activities were especially high. Comparisons of these values with published values for other Lepidoptera support the hypothesis that these enzyme systems are involved in conferring tolerance to juglone and related quinones occurring in members of the plant family Juglandaceae. Results suggest that host plant utilization by luna is more specialized at the individual or population level than at the species level and that biochemical detoxification systems may play a role in such specialization.

Key words

Actias luna Lepidoptera Saturniidae detoxification enzymes enzyme induction glutathione transferase Juglandaceae juglone nutritional ecology plant-insect interactions quinone reductase 

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References

  1. Baker, W.L. 1972. Eastern Forest Insects. U.S. Department of Agriculture, Washington, D.C.Google Scholar
  2. Brattsten, L.B. 1987a. Metabolic insecticide defenses in the boll weevil compared to those in a resistance-prone species.Pestic. Biochem. Physiol. 27:1–12.Google Scholar
  3. Brattsten, L.B. 1987b. Inducibility of metabolic insecticide defenses in boll weevils and tobacco budworm caterpillars.Pestic. Biochem. Physiol. 27:13–23.Google Scholar
  4. Brattsten, L.B., Price, S.L., andGunderson, C.A. 1980. Microsomal oxidases in midgut and fatbody tissues of a broadly herbivorous insect larva,Spodoptera eridania Cramer (Noctuidae).Comp. Biochem. Physiol. 66C:231–237.Google Scholar
  5. Cohen, E. 1986. Glutathione-S-transferase activity and its induction in several strains ofTribolium castaneum.Entomol. Exp. Appl. 41:39–44.Google Scholar
  6. Fox, L.R., andMorrow, P.A. 1981. Specialization: Species property or local phenomenon?Science 211:887–893.Google Scholar
  7. Gilbert, B.L., Baker, J.E., andNorris, D.M. 1967. Juglone (5-hydroxy-1,4-naphthoquinone) fromCarya ovata, a deterrent to feeding byScolytus multistriatus.J. Insect Physiol. 13:1453–1459.Google Scholar
  8. Gunderson, C.A., Brattsten, L.B., andFleming, J.T. 1986. Microsomal oxidase and glutathione transferase as factors influencing the effects of pulegone in southern and fall armyworm larvae.Pestic. Biochem. Physiol. 26:238–249.Google Scholar
  9. Hansen, L.G., andHodgson, E. 1971. Biochemical characteristics of insect microsomes.N- andO-demethylation.Biochem. Pharmacol. 20:1569–1578.Google Scholar
  10. Hedin, P.A., Collum, D.H., Langhans, V.E., andGraves, C.H. 1980. Distribution of juglone and related compounds in pecan and their effect onFusicladium effusum.J. Agric. Food Chem. 28:340–342.Google Scholar
  11. Holland, W.J. 1968. The Moth Book. Dover Publications, New York.Google Scholar
  12. Kapin, M.A., andAhmad, S. 1980. Esterases in larval tissues of gypsy moth,Lymantria dispar (L.): Optimum assay conditions, quantification and characterization.Insect Biochem. 10:331–337.Google Scholar
  13. Lindroth, R.L. 1988. Hydrolysis of phenolic glycosides by midgut β-glucosidases inPapilio glaucus subspecies.Insect Biochem. In press.Google Scholar
  14. Lindroth, R.L. 1989. Host plant alteration of detoxication enzyme activity inPapilio glaucus glaucus.Entomol. Exp. Appl. 50:29–35.Google Scholar
  15. Margoliash, E., andFrohwirt, N. 1959. Spectrum of horse-heart cytochromec.Biochem. J. 71:570–572.PubMedGoogle Scholar
  16. Norris, D.M. 1986. Anti-feeding compounds, pp. 97–146,in G. Haug and H. Hoffman (eds.). Chemistry of Plant Protection. 1. Sterol Biosynthesis, Inhibitors and Anti-Feeding Compounds. Springer-Verlag, New York.Google Scholar
  17. Schacterle, G.R., andPollack, R.L. 1973. A simplified method for quantitative assay of small amounts of protein in biologic material.Anal. Biochem. 51:654–655.PubMedGoogle Scholar
  18. Scriber, J.M., andFeeny, P. 1979. Growth of herbivorous caterpillars in relation to feeding specialization and to the growth form of their food plants.Ecology 60:829–850.Google Scholar
  19. Segel, I.H. 1976. Biochemical Calculations, 2nd ed. John Wiley & Sons, New York.Google Scholar
  20. Terriere, L.C. 1984. Induction of detoxication enzymes in insects.Anna. Rev. Entomol. 29:71–88.Google Scholar
  21. Tietz, H.M. 1972. An Index to the Described Life Histories, Early Stages and Hosts of the Macrolepidoptera of the Continental United States and Canada. A.C. Allyn, Sarasota, Florida.Google Scholar
  22. Wadleigh, R.W., andYu, S.J. 1987. Glutathione transferase activity of fall armyworm larvae toward α, β-unsaturated carbonyl allelochemicals and its induction by allelochemicals.Insect Biochem. 17:759–764.Google Scholar
  23. Wilkinson, L. 1987. SYSTAT: The System for Statistics. SYSTAT, Inc., Evanston, Illinois.Google Scholar
  24. Yu, S.J. 1983. Induction of detoxifying enzymes by allelochemicals and host plants in fall armyworm.Pestic. Biochem. Physiol. 9:330–336.Google Scholar
  25. Yu, S.J. 1986. Consequences of induction of foreign compound-metabolizing enzymes in insects, pp. 153–174,in L.B. Brattsten and S. Ahmad (eds.). Molecular Aspects of Insect-Plant Associations. Plenum Press, New York.Google Scholar
  26. Yu, S.J. 1987a. Quinone reductase of phytophagous insects and its induction by allelochemicals.Comp. Biochem. Physiol. 87B:621–624.Google Scholar
  27. Yu, S.J. 1987b. Biochemical defense capacity in the spined soldier bug (Podisus maculiventris) and its lepidopterous prey.Pestic. Biochem. Physiol. 28:216–223.Google Scholar

Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • Richard L. Lindroth
    • 1
  1. 1.Department of EntomologyUniversity of WisconsinMadison

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