Helicoverpa armigera

Interaction with cell membranes is also supported by recent experimental data from Barbeta et al In feeding trials using artificial diets and larvae from Helicoverpa armigera it was shown that kalata B1 has a... 

Figure 5.2 Proposed signal transduction mechanisms that stimulate the pheromone biosynthetic pathway in Helicoverpa zea and other heliothines as compared with that in Bombyx mori. It is proposed that PBAN binds to a receptor present in the cell membrane. Binding to the receptor somehow induces a receptor-activated calcium channel to open causing an influx of extracellular calcium. This calcium binds to calmodulin and in the case of B. mori will directly stimulate a phosphatase that will dephosphorylate and activate a reductase in the biosynthetic pathway. This activated reductase will then produce the pheromone bombykol. In H. zea and other heliothines like Helicoverpa armigera the calcium/calmodulin will activate adenylate cyclase to produce cAMP that will then act through kinases and/or phosphatases to stimulate acetyl-CoA carboxylase in the biosynthetic pathway.

Eliyahu D., Nagalakmish V., Kubli E. C., Choffat Y., Applebaum S. W. and Rafaeli, A. (2003) Inhibition of pheromone biosynthesis in Helicoverpa armigera by pheromonostatic peptides. J. Insect Physiol, (in press). 

Fan Y., Rafaeli A., Gileadi C. and Applebaum S. W. (1999a) Juvenile hormone induction of pheromone gland PBAN-responsiveness in Helicoverpa armigera females. Insect Biochem. Mol. Biol. 29, 635-641. 

Rafaeli A. and Gileadi C. (1995b) Modulation of the PBAN-stimulated pheromonotropic activity in Helicoverpa armigera. Insect Biochem. Mol. Biol. 25, 827-834. 

Rafaeli A., Zakarova T., Lapsker Z. and Jurenka R. A. (2003) The identification of an age-and female-specific putative PBAN membrane-receptor protein in pheromone glands of Helicoverpa armigera Possible up regulation by Juvenile Hormone. Insect Biochem. Mol. Biol. 33, 371-380. 

Zhang T., Zhang L., Xu W. and Shen J. (2001) Cloning and characterization of the cDNA of diapause hormone-pheromone biosynthesis activating neuropeptide of Helicoverpa armigera. GenBank Direct Submission. 

Helicoverpa zea Noctuoidea Noctuidae Helicoverpa armigera Noctuoidea ... 

Wang G. R. and Guo Y. Y. (2000) Cloning and expression of odorant-binding proteins from Helicoverpa armigera. Unpublished sequence, Accession Numbers AJ278991, AJ278992. 

Cunningham J. P., West S. A. and Wright D. J. (1998) Learning in the nectar foraging behaviour of Helicoverpa armigera. Ecolog. Entomol. 23, 363-369. 

Other examples of in vitro baculovirus systems (virus-cell line) are Helicoverpa armigera SNPV and Helicoverpa zea cells, with 222 polyhe-dra per cell (Lua et ah, 2002) Trichoplusia ni NPV and Trichoplmia ni cells, with 70 polyhedra per cell (Potter et ah, 1976) Lymantria dispar MNPV and Lymantria dispar cells, with 57 polyhedra per cell (Slavicek et al., 1996) Spodoptera frugiperda MNPV and Spodoptera frugiperda, with 399 polyhedra per cell (Almeida et al., 2005). 

Chakraborty S, Reid S (1999), Serial passage of a Helicoverpa armigera nucleopolyhedrovirus in Helicoverpa zea cell cultures, J. Invertebr. Pathol. 73 303-308. 

Lua LHL, Pedrini MRS, Reid S, Robertson A, Tribe DE (2002), Phenotypic and genotypic analysis of Helicoverpa armigera nucleopolyhedrovirus serially passaged in cell culture, J. Gen. Virol. 83 945-955. 

Lua LHL, Nielsen LK, Reid S (2003), Sensitivity of Helicoverpa armigera nucleopoly-hedrovirus polyhedra to sodium dodecyl sulfate, Biol. Control 26 57-67. 

Pedrini MRS, Nielsen LK, Reid S, Chan LCL (2005), Properties of a unique mutant of Helicoverpa armigera single-nucleocapsid nucleopolyhedrovirus that exhibits a partial many polyhedra and few polyhedra phenotype on extended serial passaging in suspension cell cultures, In Vitro Cell Dev. Biol. (Animal) 41 289-297. 

The antifeedant activities of all clerodanes (of natural and semisynthetic origin) have been reported in an extensive review8 covering all literature until December 2001. This review covers a total of 382 clerodanes, all tested on a variety of insect species, yet most tests are with Spodoptera species, of which S. littoralis is most often used. Other species frequently used are the CPB (L. decemlineata), Helicoverpa armigera, P. brassicae, and Ostrinia furnacalis. 

Ahmad, M., Denholm, I., and Bromilow, R.H., Delayed cuticular penetration and enhanced metabolism of deltamethrin in pyrethrin-resistant strains of Helicoverpa armigera from China and Pakistan, Pest Manag. Sci., 62, 805, 2006. 

Potent antifeedant activity against the larvae of Helicoverpa armigera has been investigated for 3-hydroxy-4-prenyl-5-methoxystilbene-2-carboxylic acid on the pod surfaces of Cajanus cajan. The activity could be modulated by quercetin-3-methyl ether [461]. 

Inhibition of Resistance-related Esterases by Piperonyl Butoxide in Helicoverpa armigera (Lepidoptera Noctuidae) and Aphis gossypti (Hemiptera Aphididae)... 

The cotton bollworm, Helicoverpa armigera, in Australia is of great economic importance and is cross-resistant to parathion-methyl and profenofos, but not to chlorpyrifos. It has an acetylcholinesterase with low sensitivity to paraoxon-methyl and profenofos, but the sensitivity to chlorpyrifos is unaltered. As Table 9.3 shows, the enzyme of the resistant insects is a little less efficient by having a slightly higher Km. (Km is the substrate concentration at which an enzyme-catalyzed reaction proceeds at one-half its maximum velocity.) This indicates a somewhat less efficient enzyme, but the difference is so slight that it does not cause any reduced fitness for the insects. The amount of and activity of acetylcholinesterase are almost always much higher than strictly necessary. 

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