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8: Mosquitocidal B. sphaericus: Toxins, Genetics, Mode of Action, Use, and Resistance Mechanisms 301 unpublished data). Further studies are required to evaluate whether strain IAB-59 is of commercial value as an alternative to B. sphaericus strains 1593, 2362, 101-B, and C3-41 (the only strains currently produced for use in the field). This depends on its potency and field performance. Additionally, several groups are currently trying to identify the genes encoding the additional toxic compounds from strains IAB-59 and LP1-G. The fact that the Bin toxin behaves as a unique moiety during the binding step indicates that the probability of selecting resistance to B. sphaericus is much higher than for Bti, which contains at least four proteins that potentially act on different target molecules. Despite reports of laboratory and field resistance, the use of B. sphaericus for the control of mosquito larvae is still of interest. Nevertheless, it is important to collect information about baseline susceptibility before starting treatment. However, as resistance to B. sphaericus is recessive, it is only possible to detect resistance when it has already become homozygous and therefore difficult to handle. Thus, it may be possible to monitor the risk of resistance development in a given area by use of molecular nucleotide probes based on the mutation of resistance genes. However, resistance to B. sphaericus seems to be very complex and different probes would be needed to cover all possible mutations, only one of which has been identified so far (Darboux et al., 2002). Both from a practical and an ecological point of view, the best and most direct way to overcome and to manage B. sphaericus resistance is of course Bti, which is already commercialised. Fortunately, all Culex populations reported to display field resistance to B. sphaericus have been tested for susceptibility to Bti. No cross-resistance has been observed. There is even some evidence for increased susceptibility in some colonies (Rao et al., 1995; Silva-Filha et al., 1995; Yuan et al., 2000). This was expected, because the multi-toxin complex of this bacterium does not share any receptor-binding sites with the B. sphaericus binary toxin (Nielsen- LeRoux and Charles, 1992). In several situations, it is recommended that Bti be used in rotation with B. sphaericus (Regis and Nielsen-LeRoux, 2000; Yuan et al., 2000). Recent results obtained in Thailand have suggested that a mixture of Bti and B. sphaericus may help reduce the risk of appearance of B. sphaericus resistance while preserving the superior field performance of B. sphaericus compared to Bti, particularly in breeding sites rich in organic matter (Mulla et al., 2003). Alternatives to natural Bti and B. sphaericus strains include genetically modified organisms, as combining different toxins binding to different receptors in the same organism is also a good way of preventing resistance. In addition to the Bin toxins, other toxins from either B. sphaericus or other insecticidal microorganisms could be produced. For example, the expression of Mtx1 genes in B. sphaericus during sporulation, i.e., under the control of a sporulation promoter, could allow the diversification of toxins. Similarly, Bti mosquitocidal toxin genes could be combined with B. sphaericus genes; some groups have already attempted this, for example by introducing the Bti genes encoding Cry4B, Cry4D or Cry11A into toxic B. sphaericus strains (Trisrisook et al., 1990; Bar et al., 1991; Poncet et al., 1994; Poncet et al., 1997). Conversely, B. sphaericus crystal toxin genes have been successfully introduced into toxic Bti (Bourgouin et al., 1990). Although these studies did not demonstrate any increase in toxicity against Anopheles and Culex, such recombinants may delay the emergence of resistant insects. Several attempts have been made to introduce or to combine toxin genes from Bti, B. thuringiensis serovar jegathesan (Bt jeg) and serovar medellin (Bt med), and to evaluate their activity towards both susceptible and B. sphaericus-resistant colonies. The introduction of Cry11A from Bti and Cry11Ba from Bt jeg partially restored the susceptibility of resistant colonies (Poncet et al., 1997; Servant et al., 1999). Nonspecific cytolytic toxins (Cyt1A and Cyt1B) also partially restored its toxicity towards two resistant colonies (Thiéry et al., 1998; Wirth et al., 2000a). A Bti strain harboring genes encoding the binary toxin as well as Cyt1 and Cry11B was more toxic than unmodified Bti IPS-82 (Park et al., 2003). Several groups have also attempted to introduce and to overproduce entomopathogenic toxins into organisms living in the environment and serving as natural foods for mosquitoes, such as cyanobacteria (Liu et al., 1996b), or to stably integrate the toxins encoding these genes into the chromosomes of other bacteria such as Enterobacter amnigenus (Tanapongpipat et al., 2003). However, given our current knowledge of B. sphaericus resistance, the expression of Bin toxin as the only active compound should be avoided. No recombinant strains have yet proved to have a better field performance than the natural strains, and no products based on recombinant strains have yet been registered for use in mosquito control programs. Therefore there is a continuing need to identify new strains with novel modes of action against the principal mosquito vectors of human diseases.
302 8: Mosquitocidal B. sphaericus: Toxins, Genetics, Mode of Action, Use, and Resistance Mechanisms References Ahmed, H.K., Mitchell, W.J., Priest, F.G., 1995. Regulation of mosquitocidal toxin synthesis in Bacillus sphaericus. Appl. Microbiol. Biotechnol. 43, 310–314. Alexander, B., Priest, F.G., 1990. Numerical classification and identification of Bacillus sphaericus including some strains pathogenic for mosquito larvae. J. Gen. Microbiol. 136, 367–376. Aquino de Muro, M., Priest, F.G., 1994. A colony hybridization procedure for the identification of mosquitocidal strains of Bacillus sphaericus on isolation plates. J. Invertebr. Pathol. 63, 310–313. Aquino de Muro, M., Mitchell, W.J., Priest, F.G., 1992. Differentiation of mosquito-pathogenic strains of Bacillus sphaericus from non-toxic varieties by ribosomal RNA gene restriction patterns. J. Gen. Microbiol. 138, 1159–1166. Arapinis, C., de la Torre, F., Szulmajster, J., 1988. Nucleotide and deduced amino acid sequence of the Bacillus sphaericus 1593M gene encoding a 51.4 kD polypeptide which acts synergistically with the 42 kD protein for expression of the larvicidal toxin. Nucleic Acids Res. 16, 7731. Bar, E., Lieman-Hurwitz, J., Rahamim, E., Keynan, A., Sandler, N., 1991. Cloning and expression of Bacillus thuringiensis israelensis d-endotoxin DNA in B. sphaericus. J. Invertebr. Pathol. 57, 149–158. Barbazan, P., Baldet, T., Darriet, F., Escaffre, H., Haman, D.D., et al., 1997. Control of Culex quinquefasciatus (Diptera: Culicidae) with Bacillus sphaericus in Maroua, Cameroon. J. Am. Mosq. Control Assoc. 13, 263–269. Baumann, L., Baumann, P., 1989. Expression in Bacillus subtilis of the 51- and 42-kilodalton mosquitocidal toxin genes of Bacillus sphaericus. Appl. Environ. Microbiol. 55, 252–253. Baumann, L., Baumann, P., 1991. Effects of components of the Bacillus sphaericus toxin on mosquito larvae and mosquito-derived tissue culture-grown cells. Curr. Microbiol. 23, 51–57. Baumann, P., Baumann, L., Bowditch, R.D., Broadwell, A.H., 1987. Cloning of the gene of the larvicidal toxin of Bacillus sphaericus 2362: evidence for a family of related sequences. J. Bacteriol. 169, 4061–4067. Baumann, L., Broadwell, A.H., Baumann, P., 1988. Sequence analysis of the mosquitocidal toxin genes encoding 51.4- and 41.9-kilodalton proteins from Bacillus sphaericus 2362 and 2297. J. Bacteriol. 170, 2045–2050. Baumann, P., Clark, M.A., Baumann, L., Broadwell, A.H., 1991. Bacillus sphaericus as a mosquito pathogen: properties of the organism and its toxins. Microbiol. Rev. 55, 425–436. Baumann, P., Unterman, B.M., Baumann, L., Broadwell, A.H., Abbene, S.J., et al., 1985. Purification of the larvicidal toxin of Bacillus sphaericus and evidence for high-molecular-weight precursors. J. Bacteriol. 163, 738–747. Becker, N., 2000. Bacterial control of vector-mosquitoes and black flies. In: Charles, J.-F., Delécluse, A., Nielsen- LeRoux, C. (Eds.), Entomopathogenic Bacteria: from Laboratory to Field Application. Kluwer Academic Publisher, Dordrecht, Boston, London, pp. 383–398. Berry, C., Hindley, J., 1987. Bacillus sphaericus strain 2362: identification and nucleotide sequence of the 41.9 kDa toxin gene. Nucleic Acids Res. 15, 5591. Berry, C., Hindley, J., Ehrhardt, A.F., Grounds, T., de Souza, I., et al., 1993. Genetic determinants of host ranges of Bacillus sphaericus mosquito larvicidal toxins. J. Bacteriol. 175, 510–518. Berry, C., Jackson-Yap, J., Oei, C., Hindley, J., 1989. Nucleotide sequence of two toxin genes from Bacillus sphaericus IAB59: sequence comparisons between five highly toxinogenic strains. Nucleic Acids Res. 17, 7516. Bourgouin, C., Delécluse, A., de la Torre, F., Szulmajster, J., 1990. Transfer of the toxin protein genes of Bacillus sphaericus into Bacillus thuringiensis subsp. israelensis and their expression. Appl. Environ. Microbiol. 56, 340–344. Broadwell, A.H., Baumann, P., 1986. Sporulationassociated activation of Bacillus sphaericus larvicide. Appl. Environ. Microbiol. 52, 758–764. Broadwell, A.H., Baumann, P., 1987. Proteolysis in the gut of mosquito larvae results in further activation of the Bacillus sphaericus toxin. Appl. Environ. Microbiol. 53, 1333–1337. Broadwell, A.H., Baumann, L., Baumann, P., 1990a. Larvicidal properties of the 42 and 51 kilodalton Bacillus sphaericus proteins expressed in different bacterial hosts: evidence for a binary toxin. Curr. Microbiol. 21, 361–366. Broadwell, A.H., Clark, M.A., Baumann, L., Baumann, P., 1990b. Construction by site-directed mutagenesis of a 39-kilodalton mosquitocidal protein similar to the larvaprocessed toxin of Bacillus sphaericus 2362. J. Bacteriol. 172, 4032–4036. Charles, J.-F., 1987. Ultrastructural midgut events in Culicidae larvae fed with Bacillus sphaericus 2297 spore/ crystal complex. Ann. Inst. Pasteur/Microbiol. 138, 471–484. Charles, J.-F., de Barjac, H., 1981. Variation du pH de l’intestin moyen d’Aedes aegypti en relation avec l’intoxication par les cristaux de Bacillus thuringiensis var. israelensis (sérotype H 14). Bull. Soc. Path. Exot. 74, 91–95. Charles, J.-F., Nicolas, L., 1986. Recycling of Bacillus sphaericus 2362 in mosquito larvae: a laboratory study. Ann. Inst. Pasteur/Microbiol. 137B, 101–111. Charles, J.-F., Hamon, S., Baumann, P., 1993. Inclusion bodies and crystals of Bacillus sphaericus mosquitocidal proteins expressed in various bacterial hosts. Res. Microbiol. 144, 411–416. Charles, J.-F., Nielsen-LeRoux, C., Delécluse, A., 1996. Bacillus sphaericus toxins: molecular biology and mode of action. Annu. Rev. Entomol. 41, 389–410. Charles, J.-F., Kalfon, A., Bourgouin, C., de Barjac, H., 1988. Bacillus sphaericus asporogenous mutants:
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INSECT CONTROL BIOLOGICAL AND SYNTH
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INSECT CONTROL BIOLOGICAL AND SYNTH
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CONTENTS Preface vii Contributors i
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PREFACE When Elsevier published the
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J T Andaloro E. I. Du Pont de Nemou
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1 Pyrethroids B P S Khambay and P J
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activity. In contrast to most other
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Figure 1 Commercial and novel pyret
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Figure 2 Pyrethroids referred to in
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4-position result in almost complet
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and their primary site of action is
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Figure 4 Folded and extended confor
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aromatic rings or methyl groups by
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pyrethroids) and consequently a sec
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1998), although the precise mechani
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polymorphisms in the protein. Of th
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observed resistance to pyrethroids,
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propoxur against Culex quinquefasci
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esistance in house fly. Insect Bioc
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Shan, G.M., Hammock, B.D., 2001. De
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A1.4. Resistance The increasing num
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B A IIS4-S5 linker, IIS5 helix and
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2 Indoxacarb and the Sodium Channel
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Figure 2 Structures of pyrazoline-l
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observed that both indoxacarb and i
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deflections resulting from stresses
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Figure 8 Dihydropyrazole block appe
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potential conduction in the CNS of
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known to affect blocker affinity, w
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Figure 13 Diagrammatic representati
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that the probable mechanism of ovil
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conventional chemistries and spinos
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Clare, J.J., Tate, S.N., Nobbs, M.,
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Tsurubuchi, Y., Karasawa, A., Nagat
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R1 N N O N H indoxacarb. Thus, whil
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3 Neonicotinoid Insecticides P Jesc
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esidues, like the pyrid-3-ylmethyl
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containing neonicotinoids, and neon
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Studies were also done using compar
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Becke, 1988; Klamt, 1995) level of
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sampling using forcefield methods (
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Figure 9 Stable conformations and p
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Figure 13 Binding to putative catio
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Figure 14 Systemicity of neonicotin
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site (Kayser et al., 2002). Clothia
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Figure 20 Important pest insects ta
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Barley yellow dwarf virus vectors s
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investigate the mode of action of n
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within the desensitized state over
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the accumulation of this acid in th
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3.8.1. Safety Profile The introduct
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Table 7 Environmental profile of co
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substance is bound irreversibly to
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imidacloprid conferring a high leve
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nAChR are comparable to the efficac
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Figure 25 Flea control achieved wit
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and the resolution of FAD was teste
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Brown, J.K., Perring, T.M., Cooper,
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In: Ishaaya, I. (Ed.), Biochemical
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Léna, C., Changeux, J.-P., 1993. A
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patterns in Colorado potato beetle
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nach Saatgutbeizung. Pflanzenschutz
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Today, photoaffinity labeling (e.g.
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for control of stinkbugs in soybean
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Biochem. Physiol., doi: 10.1016/j.p
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4 Insect Growth- and Development-Di
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The molting process is initiated by
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Table 1 Bisacylhydrazine insecticid
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4.2.2. Bisacylhydrazines as Tools o
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to the three EcRs with either muris
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of action of ecdysone agonists was
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thus inducing effects and symptomol
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and microsomes. Subsequently, Willi
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dipteran insects, like the midge, C
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eetle (Exomala orientalis) when app
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metabolic fate studies showed the i
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y specific proteins in signaling pa
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their reduced risk for the environm
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can be reversed by applying JH. JH
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door for a more rational approach t
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apparent that it was a bHLH-PAS and
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Table 9 Continued Bemisia tabaci (s
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Table 11 Insect control with some a
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Table 13 Ecotoxicological profile o
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Flucycloxuron Nonsystemic acaricide
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The discovery of diflubenzuron spaw
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Table 15 Environmental effects of s
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ecessive (R male S female) manner,
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esistance management programs due t
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IPS Paraconfusus lanier (Coleoptera
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larvae parasitized by Microplitis r
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Kostyukovsky, M., Chen, B., Atsmi,
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Three-dimensional quantitative stru
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Riddiford, L.M., 1994. Cellular and
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characterization of resistant clone
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Biological Approaches to Pest Contr
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M389 L308 M272 T304 T393 V404 L420
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5 Azadirachtin, a Natural Product i
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and Hemiptera and was related to ef
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eported, but this is rather nonspec
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important source of pest control at
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effects with physiological effects
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eing associated with an accumulatio
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et al., 1992). Salehzadeh et al. (2
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ehavior of Spodoptera littoralis (p
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indica A. Juss. IBH Publishing Comp
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Smith, S.L., Mitchell, M.J., 1988.
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which interact directly with azadir
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6 The Spinosyns: Chemistry, Biochem
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Table 1 Structures of the spinosyns
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Table 2 Biological activity of spin
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A large synthetic effort has gone i
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216 6: The Spinosyns: Chemistry, Bi
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Figure 4 Spinosad metabolism in avi
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A6 Addendum: The Spinosyns T C Spar
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246 A6: Addendum Scott, 2008) and i
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248 7: Bacillus thuringiensis: Mech
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Page 295 and 296: Table 1 Comparative properties of s
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352 10: Genetically Modified Baculo
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384 A10: Addendum cysteine protease
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This page intentionally left blank
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388 11: Entomopathogenic Fungi and
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Zare, R., Gams, W., Culham, A., 200
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434 A11: Addendum although a number
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436 A11: Addendum Examination of ge
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440 12: Insect Transformation for U
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448 A12: Addendum genetic transform
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452 Subject Index Aphis gossypii (c
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454 Subject Index Bisacylhydrazine
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456 Subject Index Cry toxins (conti
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458 Subject Index Entomopathogenic
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460 Subject Index Homoptera molting
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462 Subject Index Kinoprene (ENSTAR
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464 Subject Index Muscle(s) sodium
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466 Subject Index Photorhabdus (con
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468 Subject Index Sodium channel bl
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470 Subject Index Toxocara cati, im
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