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Volumn 109, Issue 25, 2012, Pages

Single amino acid mutation in an ATP-binding cassette transporter gene causes resistance to Bt toxin Cry1Ab in the silkworm, Bombyx mori

Author keywords

Genome; Linkage analysis; Map based cloning; PiggyBac; Toxin binding

Indexed keywords

ABC TRANSPORTER; AMINO ACID; CRY1AB TOXIN; INTESTINE ENZYME; MULTIDRUG RESISTANCE PROTEIN 4; PROTOXIN; TYROSINE;

EID: 84862509616     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1120698109     Document Type: Article
Times cited : (202)

References (46)
  • 1
    • 0022391579 scopus 로고
    • Insect resistance to the biological insecticide Bacillus thuringiensis
    • McGaughey WH (1985) Insect resistance to the biological insecticide Bacillus thuringiensis. Science 229:193-195.
    • (1985) Science , vol.229 , pp. 193-195
    • McGaughey, W.H.1
  • 3
    • 72449132872 scopus 로고    scopus 로고
    • Field-evolved insect resistance to Bt crops: Definition, theory, and data
    • Tabashnik BE, Van Rensburg JBJ, Carrière Y (2009) Field-evolved insect resistance to Bt crops: definition, theory, and data. J Econ Entomol 102:2011-2025.
    • (2009) J Econ Entomol , vol.102 , pp. 2011-2025
    • Tabashnik, B.E.1    Van Rensburg, J.B.J.2    Carrière, Y.3
  • 4
    • 51249121783 scopus 로고    scopus 로고
    • How to cope with insect resistance to Bt toxins?
    • Bravo A, Soberón M (2008) How to cope with insect resistance to Bt toxins? Trends Biotechnol 26:573-579.
    • (2008) Trends Biotechnol , vol.26 , pp. 573-579
    • Bravo, A.1    Soberón, M.2
  • 5
    • 34250617482 scopus 로고    scopus 로고
    • The diversity of Bt resistance genes in species of Lepidoptera
    • Heckel DG, et al. (2007) The diversity of Bt resistance genes in species of Lepidoptera. J Invertebr Pathol 95:192-197.
    • (2007) J Invertebr Pathol , vol.95 , pp. 192-197
    • Heckel, D.G.1
  • 6
    • 38349057537 scopus 로고    scopus 로고
    • Genetic mapping of Bt-toxin binding proteins in a Cry1A-toxin resistant strain of diamondback moth Plutella xylostella
    • Baxter SW, Zhao JZ, Shelton AM, Vogel H, Heckel DG (2008) Genetic mapping of Bt-toxin binding proteins in a Cry1A-toxin resistant strain of diamondback moth Plutella xylostella. Insect Biochem Mol Biol 38:125-135.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 125-135
    • Baxter, S.W.1    Zhao, J.Z.2    Shelton, A.M.3    Vogel, H.4    Heckel, D.G.5
  • 7
    • 78650708942 scopus 로고    scopus 로고
    • An ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxin
    • Gahan LJ, Pauchet Y, Vogel H, Heckel DG (2010) An ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxin. PLoS Genet 6: e1001248.
    • (2010) PLoS Genet , vol.6
    • Gahan, L.J.1    Pauchet, Y.2    Vogel, H.3    Heckel, D.G.4
  • 8
    • 33744454449 scopus 로고    scopus 로고
    • Construction of a single nucleotide polymorphism linkage map for the silkworm, Bombyx mori, based on bacterial artificial chromosome end sequences
    • Yamamoto K, et al. (2006) Construction of a single nucleotide polymorphism linkage map for the silkworm, Bombyx mori, based on bacterial artificial chromosome end sequences. Genetics 173:151-161.
    • (2006) Genetics , vol.173 , pp. 151-161
    • Yamamoto, K.1
  • 9
    • 46249126686 scopus 로고    scopus 로고
    • A BAC-based integrated linkage map of the silkworm Bombyx mori
    • Yamamoto K, et al. (2008) A BAC-based integrated linkage map of the silkworm Bombyx mori. Genome Biol 9:R21.
    • (2008) Genome Biol , vol.9
    • Yamamoto, K.1
  • 10
    • 84862509355 scopus 로고    scopus 로고
    • A novel single resistant gene against BT-toxin in the silkworm Bombyx mori, was located at the molecular genetic map based on RFLP
    • eds Binh ND, Akhurst RJ, Dean DH (Science and Technics, Hanoi, Vietnam)
    • Hara W, Miyamoto K, Yonsun K, Kanda K (2005) A novel single resistant gene against BT-toxin in the silkworm Bombyx mori, was located at the molecular genetic map based on RFLP. Biotechnology of Bacillus thuringiensis,, eds Binh ND, Akhurst RJ, Dean DH (Science and Technics, Hanoi, Vietnam), Vol. 5, pp 271-276.
    • (2005) Biotechnology of Bacillus Thuringiensis , vol.5 , pp. 271-276
    • Hara, W.1    Miyamoto, K.2    Yonsun, K.3    Kanda, K.4
  • 11
    • 80053969289 scopus 로고    scopus 로고
    • Parallel evolution of Bacillus thuringiensis toxin resistance in lepidoptera
    • Baxter SW, et al. (2011) Parallel evolution of Bacillus thuringiensis toxin resistance in lepidoptera. Genetics 189:675-679.
    • (2011) Genetics , vol.189 , pp. 675-679
    • Baxter, S.W.1
  • 12
    • 59649116641 scopus 로고    scopus 로고
    • The genome of a lepidopteran model insect, the silkworm Bombyx mori
    • International Silkworm Genome Consortium
    • International Silkworm Genome Consortium (2008) The genome of a lepidopteran model insect, the silkworm Bombyx mori. Insect Biochem Mol Biol 38:1036-1045.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 1036-1045
  • 13
    • 5144229657 scopus 로고    scopus 로고
    • The genome sequence of silkworm, Bombyx mori
    • Mita K, et al. (2004) The genome sequence of silkworm, Bombyx mori. DNA Res 11: 27-35.
    • (2004) DNA Res , vol.11 , pp. 27-35
    • Mita, K.1
  • 14
    • 10344265019 scopus 로고    scopus 로고
    • A draft sequence for the genome of the domesticated silkworm (Bombyx mori)
    • Biology Analysis Group
    • Xia QY, et al.; Biology Analysis Group (2004) A draft sequence for the genome of the domesticated silkworm (Bombyx mori). Science 306:1937-1940.
    • (2004) Science , vol.306 , pp. 1937-1940
    • Xia, Q.Y.1
  • 15
    • 70449713661 scopus 로고    scopus 로고
    • KAIKObase: An integrated silkworm genome database and data mining tool
    • Shimomura M, et al. (2009) KAIKObase: an integrated silkworm genome database and data mining tool. BMC Genomics 10:486.
    • (2009) BMC Genomics , vol.10 , pp. 486
    • Shimomura, M.1
  • 16
    • 0028907322 scopus 로고
    • Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis
    • Vadlamudi RK, Weber E, Ji I, Ji TH, Bulla LA, Jr. (1995) Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis. J Biol Chem 270: 5490-5494.
    • (1995) J Biol Chem , vol.270 , pp. 5490-5494
    • Vadlamudi, R.K.1    Weber, E.2    Ji, I.3    Ji, T.H.4    Bulla Jr., L.A.5
  • 17
    • 77953911945 scopus 로고    scopus 로고
    • Study of the aminopeptidase N gene family in the lepidopterans Ostrinia nubilalis (Hübner) and Bombyx mori (L.): Sequences, mapping and expression
    • Crava CM, et al. (2010) Study of the aminopeptidase N gene family in the lepidopterans Ostrinia nubilalis (Hübner) and Bombyx mori (L.): Sequences, mapping and expression. Insect Biochem Mol Biol 40:506-515.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 506-515
    • Crava, C.M.1
  • 18
    • 0029027032 scopus 로고
    • Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin
    • Knight PJK, Knowles BH, Ellar DJ (1995) Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin. J Biol Chem 270:17765-17770.
    • (1995) J Biol Chem , vol.270 , pp. 17765-17770
    • Knight, P.J.K.1    Knowles, B.H.2    Ellar, D.J.3
  • 19
    • 0242496375 scopus 로고    scopus 로고
    • Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions
    • Griffitts JS, et al. (2003) Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions. J Biol Chem 278:45594-45602.
    • (2003) J Biol Chem , vol.278 , pp. 45594-45602
    • Griffitts, J.S.1
  • 20
    • 0033886109 scopus 로고    scopus 로고
    • Bacillus thuringiensis (Bt) toxin susceptibility and isolation of resistance mutants in the nematode Caenorhabditis elegans
    • Marroquin LD, Elyassnia D, Griffitts JS, Feitelson JS, Aroian RV (2000) Bacillus thuringiensis (Bt) toxin susceptibility and isolation of resistance mutants in the nematode Caenorhabditis elegans. Genetics 155:1693-1699.
    • (2000) Genetics , vol.155 , pp. 1693-1699
    • Marroquin, L.D.1    Elyassnia, D.2    Griffitts, J.S.3    Feitelson, J.S.4    Aroian, R.V.5
  • 21
    • 3242877290 scopus 로고    scopus 로고
    • Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae
    • Jurat-Fuentes JL, Adang MJ (2004) Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae. Eur J Biochem 271: 3127-3135.
    • (2004) Eur J Biochem , vol.271 , pp. 3127-3135
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 22
    • 40549135633 scopus 로고    scopus 로고
    • Bombyx mori midgut membrane protein P252, which binds to Bacillus thuringiensis Cry1A, is a chlorophyllide-binding protein, and the resulting complex has antimicrobial activity
    • Pandian GN, et al. (2008) Bombyx mori midgut membrane protein P252, which binds to Bacillus thuringiensis Cry1A, is a chlorophyllide-binding protein, and the resulting complex has antimicrobial activity. Appl Environ Microbiol 74:1324-1331.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1324-1331
    • Pandian, G.N.1
  • 23
    • 77953974425 scopus 로고    scopus 로고
    • An alpha-amylase is a novel receptor for Bacillus thuringiensis ssp. israelensis Cry4Ba and Cry11Aa toxins in the malaria vector mosquito Anopheles albimanus (Diptera: Culicidae)
    • Fernandez-Luna MT, et al. (2010) An alpha-amylase is a novel receptor for Bacillus thuringiensis ssp. israelensis Cry4Ba and Cry11Aa toxins in the malaria vector mosquito Anopheles albimanus (Diptera: Culicidae). Environ Microbiol 12:746-757.
    • (2010) Environ Microbiol , vol.12 , pp. 746-757
    • Fernandez-Luna, M.T.1
  • 24
    • 75949112991 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis
    • Cancino-Rodezno A, et al. (2010) The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis. Insect Biochem Mol Biol 40:58-63.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 58-63
    • Cancino-Rodezno, A.1
  • 25
    • 0018962684 scopus 로고
    • Purification of the insecticidal toxin in crystals of Bacillus thuringiensis
    • Lilley M, Ruffell RN, Somerville HJ (1980) Purification of the insecticidal toxin in crystals of Bacillus thuringiensis. J Gen Microbiol 118:1-11.
    • (1980) J Gen Microbiol , vol.118 , pp. 1-11
    • Lilley, M.1    Ruffell, R.N.2    Somerville, H.J.3
  • 26
    • 0030764154 scopus 로고    scopus 로고
    • Proteinase-mediated insect resistance to Bacillus thuringiensis toxins
    • Oppert B, Kramer KJ, Beeman RW, Johnson D, McGaughey WH (1997) Proteinase-mediated insect resistance to Bacillus thuringiensis toxins. J Biol Chem 272: 23473-23476.
    • (1997) J Biol Chem , vol.272 , pp. 23473-23476
    • Oppert, B.1    Kramer, K.J.2    Beeman, R.W.3    Johnson, D.4    McGaughey, W.H.5
  • 27
    • 0347622766 scopus 로고    scopus 로고
    • Targeted gene expression using the GAL4/UAS system in the silkworm Bombyx mori
    • Imamura M, et al. (2003) Targeted gene expression using the GAL4/UAS system in the silkworm Bombyx mori. Genetics 165:1329-1340.
    • (2003) Genetics , vol.165 , pp. 1329-1340
    • Imamura, M.1
  • 28
    • 44949166820 scopus 로고    scopus 로고
    • Deletion of a gene encoding an amino acid transporter in the midgut membrane causes resistance to a Bombyx parvo-like virus
    • Ito K, et al. (2008) Deletion of a gene encoding an amino acid transporter in the midgut membrane causes resistance to a Bombyx parvo-like virus. Proc Natl Acad Sci USA 105:7523-7527.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7523-7527
    • Ito, K.1
  • 29
    • 0033988156 scopus 로고    scopus 로고
    • Germline transformation of the silkworm Bombyx mori L. using a piggyBac transposon-derived vector
    • Tamura T, et al. (2000) Germline transformation of the silkworm Bombyx mori L. using a piggyBac transposon-derived vector. Nat Biotechnol 18:81-84.
    • (2000) Nat Biotechnol , vol.18 , pp. 81-84
    • Tamura, T.1
  • 30
    • 0032879904 scopus 로고    scopus 로고
    • MRP4: A previously unidentified factor in resistance to nucleoside- based antiviral drugs
    • Schuetz JD, et al. (1999) MRP4: A previously unidentified factor in resistance to nucleoside- based antiviral drugs. Nat Med 5:1048-1051.
    • (1999) Nat Med , vol.5 , pp. 1048-1051
    • Schuetz, J.D.1
  • 31
    • 0028291484 scopus 로고
    • The receptor for Bacillus thuringiensis CrylA (c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N
    • Knight PJK, Crickmore N, Ellar DJ (1994) The receptor for Bacillus thuringiensis CrylA (c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N. Mol Microbiol 11:429-436.
    • (1994) Mol Microbiol , vol.11 , pp. 429-436
    • Knight, P.J.K.1    Crickmore, N.2    Ellar, D.J.3
  • 32
    • 41349107158 scopus 로고    scopus 로고
    • Multidrug resistance protein 4 (MRP4/ABCC4): A versatile efflux transporter for drugs and signalling molecules
    • Russel FGM, Koenderink JB, Masereeuw R (2008) Multidrug resistance protein 4 (MRP4/ABCC4): A versatile efflux transporter for drugs and signalling molecules. Trends Pharmacol Sci 29:200-207.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 200-207
    • Russel, F.G.M.1    Koenderink, J.B.2    Masereeuw, R.3
  • 33
    • 0037434835 scopus 로고    scopus 로고
    • A cadherin-like protein functions as a receptor for Bacillus thuringiensis Cry1Aa and Cry1Ac toxins on midgut epithelial cells of Bombyx mori larvae
    • Hara H, et al. (2003) A cadherin-like protein functions as a receptor for Bacillus thuringiensis Cry1Aa and Cry1Ac toxins on midgut epithelial cells of Bombyx mori larvae. FEBS Lett 538:29-34.
    • (2003) FEBS Lett , vol.538 , pp. 29-34
    • Hara, H.1
  • 34
    • 0037157109 scopus 로고    scopus 로고
    • Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella - Their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin
    • Nakanishi K, et al. (2002) Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella - their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin. FEBS Lett 519:215-220.
    • (2002) FEBS Lett , vol.519 , pp. 215-220
    • Nakanishi, K.1
  • 35
    • 34547483580 scopus 로고    scopus 로고
    • Carotenoid silk coloration is controlled by a carotenoid-binding protein, a product of the Yellow blood gene
    • Sakudoh T, et al. (2007) Carotenoid silk coloration is controlled by a carotenoid-binding protein, a product of the Yellow blood gene. Proc Natl Acad Sci USA 104: 8941-8946.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8941-8946
    • Sakudoh, T.1
  • 36
    • 0032266986 scopus 로고    scopus 로고
    • Effect of the carboxyl-terminal protein of Cry1Ab in Bacillus thuringiensis on toxicity against the silkworm, Bombyx mori
    • Kim YS, Kanda K, Kato F, Murata A (1998) Effect of the carboxyl-terminal protein of Cry1Ab in Bacillus thuringiensis on toxicity against the silkworm, Bombyx mori. Appl Entomol Zool (Jpn) 33:473-477.
    • (1998) Appl Entomol Zool (Jpn) , vol.33 , pp. 473-477
    • Kim, Y.S.1    Kanda, K.2    Kato, F.3    Murata, A.4
  • 37
    • 0026760525 scopus 로고
    • Location of a Bombyx mori receptor binding region on a Bacillus thuringiensis delta-endotoxin
    • Lee MK, Milne RE, Ge AZ, Dean DH (1992) Location of a Bombyx mori receptor binding region on a Bacillus thuringiensis delta-endotoxin. J Biol Chem 267: 3115-3121.
    • (1992) J Biol Chem , vol.267 , pp. 3115-3121
    • Lee, M.K.1    Milne, R.E.2    Ge, A.Z.3    Dean, D.H.4
  • 39
    • 0002442490 scopus 로고
    • Use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis to qantify Bacillus thuringiensis delta-endotoxins
    • eds Hickele LA, Fitch WL American Chemical Society, Washington, DC
    • Brussock SM, Currier TC (1990) Use of sodium dodecyl sulfate- polyacrylamide gel electrophoresis to qantify Bacillus thuringiensis delta-endotoxins. Analytical Chemistry of Bacillus thuringiensis, eds Hickele LA, Fitch WL (American Chemical Society, Washington, DC), pp 78-87.
    • (1990) Analytical Chemistry of Bacillus thuringiensis , pp. 78-87
    • Brussock, S.M.1    Currier, T.C.2
  • 40
    • 33744955805 scopus 로고    scopus 로고
    • Binding of Cry1Ab toxin, a Bacillus thuringiensis insecticidal toxin, to proteins of the bovine intestinal epithelial cell: An in vitro study
    • Shimada N, Miyamoto K, Kanda K, Murata H (2006) Binding of Cry1Ab toxin, a Bacillus thuringiensis insecticidal toxin, to proteins of the bovine intestinal epithelial cell: An in vitro study. Appl Entomol Zool (Jpn) 41:295-301.
    • (2006) Appl Entomol Zool (Jpn) , vol.41 , pp. 295-301
    • Shimada, N.1    Miyamoto, K.2    Kanda, K.3    Murata, H.4
  • 41
    • 85007720702 scopus 로고
    • Processing of delta endotoxin from Bacillus thuringiensis subspp. Kurstaki HD-1 and HD-73 by immobilized trypsin and chymotrypsin
    • Indrasith L, et al. (1991) Processing of delta endotoxin from Bacillus thuringiensis subspp. Kurstaki HD-1 and HD-73 by immobilized trypsin and chymotrypsin. Appl Entomol Zool (Jpn) 26:485-492.
    • (1991) Appl Entomol Zool (Jpn) , vol.26 , pp. 485-492
    • Indrasith, L.1
  • 42
    • 45949125218 scopus 로고
    • Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae)
    • Wolfersberger M, et al. (1987) Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae). Comp Biochem Physiol A Physiol (Bethesda) 86:301-308.
    • (1987) Comp Biochem Physiol A Physiol (Bethesda) , vol.86 , pp. 301-308
    • Wolfersberger, M.1
  • 43
    • 0010611602 scopus 로고
    • No crossing over in the female of the silkworm moth
    • Sturtevant AH (1915) No crossing over in the female of the silkworm moth. Am Nat 49:42-44.
    • (1915) Am Nat , vol.49 , pp. 42-44
    • Sturtevant, A.H.1
  • 44
    • 33744456105 scopus 로고
    • A study of Mendelian factors in the silkworm, Bombyx mori
    • Tanaka Y (1913) A study of Mendelian factors in the silkworm, Bombyx mori. J Coll Agric Tohoku Imp Univ 5:91-113.
    • (1913) J Coll Agric Tohoku Imp Univ , vol.5 , pp. 91-113
    • Tanaka, Y.1
  • 45
    • 33748527167 scopus 로고    scopus 로고
    • Evaluating promoter sequences for trapping an enhancer activity in the silkworm Bombyx mori
    • Uchino K, et al. (2006) Evaluating promoter sequences for trapping an enhancer activity in the silkworm Bombyx mori. J Insect Biotechnol Sericol 75:89-97.
    • (2006) J Insect Biotechnol Sericol , vol.75 , pp. 89-97
    • Uchino, K.1
  • 46
    • 0142027812 scopus 로고    scopus 로고
    • Juvenile hormone acid methyltransferase: A key regulatory enzyme for insect metamorphosis
    • Shinoda T, Itoyama K (2003) Juvenile hormone acid methyltransferase: A key regulatory enzyme for insect metamorphosis. Proc Natl Acad Sci USA 100:11986-11991.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11986-11991
    • Shinoda, T.1    Itoyama, K.2


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