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NTIS 바로가기한국응용곤충학회지 = Korean journal of applied entomology, v.54 no.1, 2015년, pp.7 - 15
김영태 (안동대학교 생명자원과학과) , 김은성 (안동대학교 생명자원과학과) , 박영진 (안동대학교 생명자원과학과) , 김용균 (안동대학교 생명자원과학과)
CpBV (Cotesia plutellae bracovirus) is a polydnavirus and encodes a cystatin (CpBV-CST1) gene. Its overexpression suppresses insect immunity and alters insect developmental processes. This study aimed to construct a genetically modified (GM) tobacco to further explore the physiological function of t...
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핵심어 | 질문 | 논문에서 추출한 답변 |
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프루텔고치벌은 무엇을 통해 배추좀나방의 면역 및 발육을 억제하는가? | 특별히 내부기생봉이 가지고있는 기생인자 가운데 폴리드나바이러스는 곤충의 면역 및 발육을 억제하는 다수의 유전인자를 보유하고 있다(Kim, 2006). 국내에 서식하는 프루텔고치벌(Cotesia plutellae)은 자신의 공생 바이러스인 CpBV (Cotesia plutellae bracovirus)를 통해 기주인 배추좀나방(Plutella xylostella)의 면역 및 발육을 억제한다(Kim et al., 2007). | |
CpBV 바이러스 게놈은 몇 개의 시스타틴 유전자를 가지고 있는가? | CpBV가 피기생체에서 발현하는 유전자가운데 시스타틴(cystatin: CST)은 이러한 곤충생리교란 인자로서 주목받고 있다. CpBV 바이러스 게놈은 4 개의 시스타틴 유전자를 가지고 있으며, 이 가운데 3 개가 피기생체에서 발현된다고 보고되었다(Kim et al., 2013). | |
식물형질전환 방법은 무엇이 있는가? | 현재 이용되고 있는 식물형질전환 기술은 기존의 교잡육종이나 조직배양에서 불가능했던 유전형질을 단시간에 도입시켜 형질전환체를 확보할 수 있다. 식물체에 외래유전자를 도입하는데 주로 이용되는 형질전환 방법으로는 Ti 플라스미드나 다른 종류의 운반체를 아그로박테리움(Agrobacterium tumefasciens)과 유전자총(particle bombardment)으로 유전자를 도입시키거나, 애기장대에 주로 이용되는 화아침지(floral dip)에 의한 형질전환 등이 있다. 해충저항성을 주기 위한 작물형질전환에 이용되는 목표유전자는 기능성 단백질을 코딩하는 유전자(Portaet al. |
Agarwala, K.L., Kawabata, S., Hirata, M., Miyagi, M., Tsunasawa, S., Iwanaga, S., 1996. A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: purification, characterization, cDNA cloning, and tissue localization. J. Biochem. 119, 85-94.
Amani, J., Kazemi, R., Ali Reza Abbasi, A.R., Ali Hatef Salmanian, A.H., 2011. A simple and rapid leaf genomic DNA extraction method for polymerase chain reaction analysis. Iran. J. Biotech. 9, 69-71.
Attardo, G.M., Strickler-Dinglasan, P., Perkin, S.A.H., Caler, E., Bonaldo, M.F., Soareo, M.B., El-Sayeed, N., Aksoy, S., 2006. Analysis of fat body transcriptome from the adult tsetse fly, Glossina morsitans. Insect Mol. Biol. 15, 411-424.
Burke, G.R., Strand, M.R., 2014. Systematic analysis of a wasp parasitism arsenal. Mol. Ecol. 23, 890-901.
Carrillo, L., Martinez, M., Ramessar, K., Cambra, I., Castanera, P., Ortego, F., Diaz, I., 2011. Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases. Plant Cell Rep. 30, 101-112.
Chan, Y., Yang, A., Chen, J., Yeh, K., Chan, M., 2010. Heterologous expression of taro cystatin protects transgenic tomato against Meloidogyne incognita infection by means of interfering sex determination and suppressing gall formation. Plant Cell Rep. 29. 231-238.
Cho, W.L., Tsao, S.M Hays, A.R., Walter, R., Chen, J.S., Snigirevskaya, E.S., Raikhel, A.S., 1999. Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor. J. Biol. Chem. 274, 13311-13321.
De Gregorio, E., Spellman, P.T., Rubin, G.M., Lemaitre, B., 2001. Genome-wide analysis of the Drosophila immune response by using oligo nucleotide microarray. Proc. Natl. Acad. Sci. USA 98, 12590-12595.
Dubin, G., 2005. Proteinaceous cysteine protease inhibitors. Cell Mol. Life Sci. 62, 653-669.
Haunerland, N.H., Shirk, P.D., 1995. Regional and functional differentiation in the insect fat body. Annu. Rev. Entomol. 40, 121-145.
Hegedus, D., O'Grady, M., Chamankhah, M., Baldwin, D., Gleddie, S., Braun, L., Erlandson, M., 2002. Changes in cysteine protease activity and localization during midgut metamorphosis in the crucifers root maggots (Delia radicum). Insect Biochem. Mol. Biol. 32, 1585-1596.
Herrera-Estrella, L., Van den Broeck, G., Maenhaut, R., Van Montagu, M., Schell, J., 1984. Light-inducible and chloroplast associated expression of a chimeric gene introduced into Nicotiana tabacum using a Ti plasmid vector. Nature 310, 115-120.
Homma, K., Kurata, S., Natori, S., 1994. Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly) and its involvement in the differentiation of imaginal disc. J. Biol. Chem. 269, 15258-15264.
Kim, Y., 2006. Polydnavirus and its novel application to insect pest control. Kor. J. Appl. Entomol. 45, 241-259.
Koo, Y.D., Ahn, J.E., Salzman, R.A., Moon, J., Chi, Y.H., Yun, D.J., Lee, S.Y., Koiwa, H., Zhu-salzman, K., 2008. Functional expression of an insect cathespin B-like counter-defence protein. Insect Mol. Biol. 17, 235-245.
Kurata, S., Saito, H. Natori, S., 1992. The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga. Dev. Biol. 153, 115-121.
Lecaille, F., Kaleta, J., Bromme, D., 2002. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102, 4459-4488.
Lecardonnel, A., Chauvin, L., Jouanin, L., Beaujean, A., Prevosta, G., Sangwan-Norreeld, B., 1999. Effects of rice cystatin I expression in transgenic potato on Colorado potato beetle larvae. Plant Sci. 140, 71-79.
Levy, F., Rabel, D., Charlet, M., Bulet, P., Hoffmann, J.A., Ehret-Sabatier, L., 2004. Peptidomic and proteomic analysis of the systemic immune response of Drosophila. Biochimie 86, 607-616.
Liu, J., Shi, G.P., Zhang, W.Q., Zhang, G.R., Xy, W.H., 2006. Cathepsin L function in insect moulting: moleculoar cloning and functional analysis in cotton bollworm, Helicoverpa armigera. Insect Mol. Biol. 15, 823-834.
Livak, K.J., Schmittgen, T.D., 2001. Analysis of relative gene expression data using real-time quantitative PCR and the $2^{-{\Delta}{\Delta}CT}$ method. Methods 25, 402-408.
Murashige, T., Skoog, F., 1962. A revised medium for rapid growth and bioassays with tobacco cultures. Physiol. Plant. 15, 473-497.
Olsson, S.L., Ek, B., Bjork, I., 1999. The affinity and kinetics of inhibition of cyteine proteinases by intact recombinant bovine cystatin C. Biochim. Biophys. Acta 1432, 73-81.
Park, Y., Ahn, S., Vogel, H., Kim, Y., 2014. Integrin ${\beta}$ subunit and its RNA interference in immune and developmental processes of the Oriental tobacco budworm, Helicoverpa assulta. Dev. Comp. Immunol. 47, 59-67.
Porta, H., Jimenez, G., Cordoba, E., Leon, P., Soberon, M., Bravo, A., 2011. Tobacco plants expressing the Cry1AbMod toxin suppress tolerance to Cry1Ab toxin of Manduca sexta cadherinsilenced larvae. Insect Biochem. Mol. Biol. 41, 513-519.
Rawlings, N.D., Barrett, A.J., 1990. Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 30, 60-71.
Saito, H., Kurata, S., Natori, S., 1992. Purification and characterization of a hemocyte proteinase of Sarcophaga, possibly participating in elimination of foreign substances. Eur. J. Biochem. 209, 939-944.
Sambrook, J., Fritsh, E.F., Maniatis, T., 1989. Molecular cloning. A laboratory manual. 2nd Ed. Cold Spring Harbor Laboratory Press, NY.
Senthilkumar, R., Cheng, C.P., Yeh, K.W., 2010. Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco. Plant Biotech. J. 8, 65-75.
Shindo, T., Van Der Hoorn, R.A., 2008. Papain-like cysteine protease: key players at molecular battlefields employed by both plants and their invaders. Mol. Plant Pathol. 9, 119-125.
Smid, I., Gruden, K., Gasparic, M. B., Koruza, K., Petek, M., Pohleven, J., Brzin, J., Kos, J., Zel, J., Sabotic, J., 2013. Inhibition of the growth of Colorado potato beetle larvae by macrocypins, protease inhibitors from the parasol mushroom. J. Agric. Food Chem. 61, 12499-12509.
Tabashnik, B.E., Brevault, T., Carriere, Y., 2013. Insect resistance to Bt crops: lessons from the first billion acres. Nat. Biotech. 31, 510-521.
Uchida, K., Ohmori, D., Ueno, T., Nishizuka, M., Eshita, Y., Fukunaga, A., Kominami, E., 2001. Preoviposition activation of cathepsin-like proteinases in degenerating ovarian follicles of the mosquito Culex pipiens pallens. Dev. Biol. 237, 68-78.
Yamamoto, Y., Watabe, S., Kageyama, T., Takahashi, S., 1999. Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori. Arch. Insect Biochem. Physiol. 41, 119-129.
Zhang, Y., Lu, Y.X., Liu, J., Feng, Q.L., Xu, W.H., 2013. A regulatory pathway, ecdysone-transcription factor Relish-cathepsin L, is involved in insect fat body dissociation. PLOS Genetics 9, e1003273.
Zhou, J., Ueda, M., Umemiya, R., Battsetseg, B., Boldbaatar, D., Xuan, X., Fujisaka, K., 2006. A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity. Insect Biochem. Mol. Biol. 36, 527-535.
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