- 1) Engström, Y., Induction and regulation of antimicrobial peptides in Drosophila. Dev. Comp. Immunol., 23, 345–358 (1999).
- 2) Hoffman, J. A., Kafatos, F. C., Janeway, C. A., and Ezekowitz, R. A., Phylogenetic perspectives in innate immunity. Science, 284, 1313–1318 (1999).
- 3) Hoffmann, J. A., The immune response of Drosophila. Nature, 426, 33–38 (2003).
- 4) Hultmark, D., Drosophila immunity: paths and patterns. Curr. Opin. Immunol., 15, 12–19 (2003).
- 5) Imler, J. K., and Bulet, P., Antimicrobial peptides and activation of immune responses in Drosophila: structures, activities and gene regulation. Chem. Immunol. Allergy, 86, 1–21 (2005).
- 6) Kurata, S., Ariki, S., and Kawabata, S., Recognition of pathogens and activation of immune responses in Drosophila and horseshoe crab innate immunity. Immunobiology, 211, 237–249 (2006).
- 7) Lemaitre, B., The road to Toll. Nat. Rev. Immunol., 4, 521–527 (2004).
- 8) Morishima, I., Suginaka, S., Ueno, T., and Hirano, H., Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori. Comp. Biochem. Physiol., 95B, 551–554 (1990).
- 9) Teshima, T., Nakai, T., Ueki, Y., and Shiba, T., Structure determination of lepidopteran, self-defense factor produced by silkworm. Tetrahedron, 42, 829–834 (1986).
- 10) Teshima, T., Nakai, T., Ueki, Y., and Shiba, T., Structure determination of lepidopteran C, self-defense factor produced by silkworm (Bombyx mori). Tetrahedron, 43, 4513–4518 (1987).
- 11) Sugiyama, M., Kuniyoshi, H., Kotani, E., Taniai, K., Kato, Y., Kadono-Okuda, K., Yamamoto, M., Shimabukuro, M., Chowdhury, S., Choi, S. K., Kataoka, H., Suzuki, A., and Yamakawa, M., Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins. Insect Biochem. Mol. Biol., 25, 385–392 (1995).
- 12) Hara, S., and Yamakawa, M., Moricin, a novel antibacterial peptide, isolated from the silkworm, Bombyx mori. J. Biol. Chem., 270, 29923–29927 (1995a).
- 13) Hara, S., and Yamakawa, M., A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem. J., 310, 651–656 (1995b).
- 14) Christensen, B., Fink, J., Merrifield, R. B., and Mauzerall, D., Channel-forming properties of cecropins and related model compounds in corporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA, 85, 5072–5076 (1988).
- 15) Yamakawa, M., and Tanaka, H., Immune proteins and their gene expression in the silkworm, Bombyx mori. Dev. Comp. Immunol., 23, 281–289 (1999).
- 16) Sumida, M., Ichimori, H., Johchi, S., Takaoka, A., Yuhki, T., Mori, H., and Matsubara, F., Antibacterial activity inducible in the haemolymph of the silkworm, Bombyx mori, by injection of formalin-treated Echerichia coli K-12 during the fifth larval instar and pharate adult development. Comp. Biochem. Physiol., 101B, 165–171 (1992).
- 17) Tanaka, H., Yamamoto, M., Moriyama, Y., Yamao, M., Furukawa, S., Sagisaka, A., Nakazawa, H., Mori, H., and Yamakawa, M., A novel Rel protein and shortened isoform that differentially regulate antibacterial peptide genes in the silkworm Bombyx mori. Biochim. Biophys. Acta, 1730, 10–21 (2005).
- 18) Taniai, K., and Tomita, S., A novel lipopolysaccharide response element in the Bombyx mori cecropin B promoter. J. Biol. Chem., 275, 13179–13182 (2000).
- 19) Shimabukuro, M., Xu, J., Sugiyama, M., Taniai, K., Kadono-Okuda, K., Kato, Y., Yamamoto, M., Chowdhury, S., Choi, S. K., Choi, H. K., Miyanoshita, A., Debnath, N. C., and Yamakawa, M., Signal transduction for cecropin B gene expression in hemocytes of the silkworm, Bombyx mori. Appl. Entomol. Zool., 31, 135–143 (1996).
- 20) Kim, S. H., Park, B. S., Yun, E. Y., Je, Y. H., Woo, S. D., Kang, S. W., Kim, K. Y., and Kang, S. K., Cloning and expression of a novel gene encoding a new antibacterial peptide from silkworm, Bombyx mori. Biochem. Biophys. Res. Commun., 246, 388–392 (1998).
- 21) Axén, A., Carlsson, A., Engström, Å., and Bennich, H., Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae. Eur. J. Biochem., 247, 614–619 (1997).
- 22) Mackintosh, J. A., Gooley, A. A., Karuso, P. H., Beattie, A. J., Jardinet, D. R., and Veal, D. A., A gloverin-like antibacterial protein is synthesized in Helicoverpa armigera following bacterial challenge. Dev. Comp. Immunol., 22, 387–399 (1998).
- 23) Lundström, A., Liu, G., Kang, D., Berzins, K., and Steiner, H., Tricoplusia ni gloverin, an inducible immune gene encoding an antibacterial insect protein. Insect Biochem. Mol. Biol., 32, 795–801 (2002).
- 24) Zhu, Y., Johnson, T. J., Meyers, A. A., and Kanost, M. R., Identification by subtractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body. Insect Biochem. Mol. Biol., 33, 541–559 (2003).
- 25) Promboon, A., Shimada, T., Fujiwara, H., and Kobayashi, M., Linkage map of random amplified polymorphic DNAs (RAPDs) in the silkworm, Bombyx mori. Genet. Res. (Cambridge), 66, 1–7 (1995).
- 26) Takahashi, T., Murakami, H., Imanishi, S., Miyazaki, M., Kamiie, K., Suzuki, K., Taira, H., and Yamashita, T., Calreticulin is transiently induced after immunogen treatment in the fat body of the silkworm Bombyx mori. J. Insect Biotechnol. Sericol., 75, 79–84 (2006).
- 27) Hultmark, D., Engström, A., Bennich, H., Kapur, R., and Boman, H. G., Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur. J. Biochem., 127, 207–217 (1982).
- 28) Sugiyama, M., Kuniyoshi, H., Kotani, E., Taniai, K., Kato, Y., Kadono-Okuda, K., Yamamoto, M., Shimabukuro, M., Chowdhury, S., Choi, S. K., Kataoka, H., Suzuki, A., and Yamakawa, M., Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins. Insect Biochem. Mol. Biol., 25, 385–392 (1995).
- 29) Dickinson, L., Russell, V., and Dunn, P. E., A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. J. Biol. Chem., 263, 19424–19429 (1988).
- 30) Lidholm, D. A., Gudmundsson, G. H., Xanthopoulos, K. G., and Boman, H. G., Insect immunity: cDNA clones coding for the precursor forms of cecropins A and D, antibacterial proteins from Hyalophora cecropia. FEBS Lett., 226, 8–12 (1987).
- 31) Chowdhury, S., Taniai, K., Hara, S., Kadono-Okuda, K., Kato, K., Yamamoto, M., Xu, J., Choi, S. K., Debnath, N. C., Choi, H. K., Miyanoshita, A., Sugiyama, M., Asaoka, A., and Yamakawa, M., cDNA cloning and gene expression of lebocin, a novel member of antibacterial peptides from the silkworm, Bombyx mori. Biochim. Biophys. Res. Commun., 214, 271–278 (1995).
- 32) Furukawa, S., Taniai, K., Ishibashi, J., Hara, S., Shono, T., and Yamakawa, M., A novel member of lebocin gene family from the silkworm, Bombyx mori. Biochem. Biophys. Res. Commun., 238, 769–774 (1997).
- 33) Furukawa, S., Tanaka, H., Nakazawa, H., Ishibashi, J., Shono, T., and Yamakawa, M., Inducible gene expression of moricin, a unique antibacterial peptide from the silkworm (Bombyx mori). Biochem. J., 340, 265–271 (1999).
- 34) Taniai, K., Kato, Y., Hirochika, H., and Yamakawa, M., Isolation and nucleotide sequence of cecropin B cDNA clones from the silkworm, Bombyx mori. Biochim. Biophys. Acta, 1132, 203–206 (1992).
- 35) Leuiller, F., Parquet, C., Pili-Floury, S., Ryu, J. H., Caroff, M., Lee, W. J., Mengin-Lecreulx, D., and Lemaitre, B., The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nat. Immunol., 4, 478–484 (2003).
- 36) Werner, T., Borge-Remberg, Mellroth, P., Steiner, H., and Hultmark, D., Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan. J. Biol. Chem., 248, 26319–26322 (2003).
- 37) Kaneko, T., Goldman, W. E., Mellroth, P., Steiner, S., Fukase, K., Kusumoto, S., Harley, W., Fox, A., Golenbock, D., and Silverman, N., Monomeric and polymeric Gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity, 20, 637–649 (2004).
- 38) Taniai, K., Furukawa, S., Shono, T., and Yamakawa, M., Elicitors triggering the simultaneous gene expression of antibacterial proteins of the silkworm, Bombyx mori. Biochem. Biophys. Res. Commun., 226, 783–790 (1996).
Full access
Expression of Antimicrobial Peptide Genes Encoding Enbocin and Gloverin Isoforms in the Silkworm, Bombyx mori
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.