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Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae)

Published online by Cambridge University Press:  09 March 2007

B. Oppert ,
K. Hartzer  and
M. Zuercher
B. Oppert*
Affiliation:
USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA
K. Hartzer
Affiliation:
Department of Entomology, Kansas State University, Waters Hall, Manhattan, KS 66506, USA
M. Zuercher
Affiliation:
USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA
*
*Fax: 785 537 5584 E-mail: [email protected]
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Abstract

The cigarette beetle, Lasioderma serricorne (Fabricius), is a common pest of stored foods. A study of digestive proteinases in L. serricorne was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. Optimal casein hydrolysis by luminal proteinases of L. serricorne was in pH 8.5–9.0 buffers, although the pH of luminal contents was slightly acidic. Results from substrate and inhibitor analyses indicated that the primary digestive proteinases were serine proteinases. The most effective inhibitors of caseinolytic hydrolysis were from soybean (both Bowman Birk and Kunitz), with some inhibition by chymostatin, N-TOSYL-L-phenylalanine chloromethyl ketone, and leupeptin. Casein zymogram analysis identified at least eight proteolytic activities. Activity blot analyses indicated one major proteinase activity that hydrolysed the trypsin substrate N-α-benzoyl-L-arginine ρ-nitroanilide, and three major proteinase activities that hydrolysed the chymotrypsin substrate N-succinyl ala-ala-pro-phe ρ-nitroanilide. The absence of cysteine, aspartic, and metallo proteinases in L. serricorne digestion was evidenced by the lack of activation by thiol reagents, alkaline pH optima, and the results from class-specific proteinase inhibitors. The data suggest that protein digestion in L. serricorne is primarily dependent on trypsin- and chymotrypsin-like proteinases.

Type
Research Article
Information
Bulletin of Entomological Research , Volume 92 , Issue 4 , August 2002 , pp. 331 - 336
Copyright
Copyright © Cambridge University Press 2002

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References

Berenbaum, M. (1980) Adaptive significance of midgut pH in larval Lepidoptera. American Naturalist 115, 138–146.CrossRefGoogle Scholar
Birk, Y. (1985) The Bowman-Birk inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans. International Journal of Peptide Protein Research 25, 113–131.CrossRefGoogle ScholarPubMed
Bolognesi, R., Ribeiro, A.F., Terra, W.R. & Ferreira, C. (2001) The peritrophic membrane of Spodoptera frugiperda: secretion of peritrophins and role in immobilization and recycling digestive enzymes. Archives of Insect Biochemistry and Physiology 47, 62–75.CrossRefGoogle ScholarPubMed
Catterji, S., Sarup, P. & Bose, B.N. (1963) Lasioderma serricorne Fabricius (Coleoptera: Anobiidae) as a pest of mustard seeds in storage. Indian Oilseeds Journal 7, 287–291.Google Scholar
Eberhardt, H.-J. (1997) Alternative forms of storage protection: biological insecticides for the control of the cigarette beetle (Lasioderma serricorne) and the tobacco moth (Ephestia elutella). Beiträge zur Tabakforschung International 17, 35–51.Google Scholar
Frugoni, J.A.C. (1957) Tampone universale di Britton e Robinson a forza ionica costante. Gazetta Chimica Italiana 87, 403–407.Google Scholar
GirardC., Le C., Le, Métayer, M., Bonadé-Bottino, M., Pham-Delègue, M.-H. & Jouanin, L. (1998) High level of resistance to proteinase inhibitors may be conferred by proteolytic cleavage in beetle larvae. Insect Biochemistry and Molecular Biology 28, 229–237.CrossRefGoogle ScholarPubMed
Houseman, J.G. & Thie, N.M.R. (1993) Difference in digestive proteolysis in the stored maize beetles: Sitophilus zeamais (Coleoptera: Curculionidae) and Prostephanus truncatus (Coleoptera: Bostrichidae). Journal of Economic Entomol 86, 1049–1054.CrossRefGoogle Scholar
Howe, R.W. (1957) A laboratory study of the cigarette beetle, Lasioderma serricorne (F.) (Col., Anobiidae) with a critical review of the literature on its biology. Bulletin of Entomological Research 48, 9–58.CrossRefGoogle Scholar
Kaelin, P., Zaugg, L., Albertini, A.M. & Gadani, F. (1999) Activity of Bacillus thuringiensis isolates on Lasioderma serricorne (F.) (Coleoptera: Anobiidae). Journal of Stored Product Research 35, 145–158.CrossRefGoogle Scholar
LeCato, G.L. (1978) Infestation and development by the cigarette beetle in spices. Journal of the Georgia Entomological Society 13, 100–105.Google Scholar
Milne, D.L. (1963) A study of the nutrition of the cigarette beetle, Lasioderma serricorne F., (Coleoptera: Anobiidae) and a suggested new method for its control. Journal of the Entomological Society of South Africa 26, 43–63.Google Scholar
Oppert, B. (2000) Transgenic plants expressing enzyme inhibitors and the prospects for biopesticide development. pp 83–95. in Koul, O. & Dhaliwal, G.S., (Ed.) In Phytochemical biopesticides. The Netherlands: Harwood Academic.Google Scholar
Oppert, B. & Kramer, K.J. (1998) Economical proteinase activity blot. In American Biotechnology Laboratory 16, 20.Google Scholar
Oppert, B., Kramer, K.J., Johnson, D., Upton, S.J. & McGaughey, W.H. (1996) Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. Insect Biochemistry and Molecular Biology 26, 571–583.CrossRefGoogle ScholarPubMed
Oppert, B., Kramer, K.J. & McGaughey, W.H. (1997) Rapid microplate assay of proteinase mixtures. BioTechniques 23, 70–72.CrossRefGoogle ScholarPubMed
Oppert, B., Hartzer, K. & Smith, C.M. (2000) Characterization of the digestive proteinases of Hypera postica (Gyllenhal) (Coleoptera: Curculionidae). Transactions of the Kansas Academy of Sciences 103, 99–110.CrossRefGoogle Scholar
Pant, N.C. & Fraenkel, G. (1950) The function of the symbiotic yeasts of two insect species, Lasioderma serricorne F. and Stegobium paniceum L. Science 112, 498–500.CrossRefGoogle Scholar
Rajendran, S. & Narasimhan, K.S. (1994) Phosphine resistance in the cigarette beetle Lasioderma serricorne (Coleoptera: Anobiidae) and overcoming control failures during fumigation of stored tobacco. International Journal of Pest Management 40, 207–210.CrossRefGoogle Scholar
Richards, O.W. & Herford, G.V.B. (1930) Insects found associated with cacao, spices, and dried fruits in London warehouses. Annals of Applied Biology 17, 367–395.CrossRefGoogle Scholar
Zettler, J.L. & Arthur, F.H. (2000) Chemical control of stored product insects with fumigants and residual treatments. Crop Protection 19, 8–10.CrossRefGoogle Scholar
Zhu, Y.-C. & Baker, J.E. (1999) Characterization of midgut trypsin-like enzymes and three trypsinogen cDNAs from the lesser grain borer, Rhyzopertha dominica (Coleoptera: Bostrichidae). Insect Biochemistry and Molecular Biology 29, 1053–1063.CrossRefGoogle ScholarPubMed