Susceptibilities of two populations of Aphis gossiper Glover to selected insecticides

Two populations of Aphis gossypii were collected from cotton and melon crops treated with insecticides to control this aphid species. The  susceptibility of both aphid populations to pymetrozine, Pirimicarb, Oxydemeton-methyl and Imidacloprid was evaluated using leaf deep bioassays in Laboratory which were commonly used to control this aphid on both crops. Results showed that LC50 values of these insecticides against clones of cotton aphid were 452, 1427, 1810 and 209 ppm, respectively. LC50 values of the above mentioned pesticides against clones of melon aphid were 625, 688, 523 and 125 ppm, respectively. Lc50 data showed that aphids reared on melon was 2.07, 1.6 and 3.4 times more susceptible than cotton aphids to Pirimicarb, Imidaclopride and Oxydemeton-methyl and 1.4 times more resistant to Pymetrozine, respectively. In conclusion, it has been shown that clones of cotton aphid is on average 3.4-fold less susceptible to Oxydemeton- methyl, 2-fold less susceptible to pirimicarb, 1.6-fold less susceptible to Imidacloprid and nearly 0.7-fold more   susceptible to pymetrozine than clones of melon aphid. There was little difference in susceptibility to pymetrozine between the two populations. It is also suggested that continuous resistance monitoring should be conducted on a regional scale to identify the efficiency of compounds which are applied against this insect species.Key words: Aphis gossypii, cotton, melon, insecticide resistance

Effect of plant seeds protein extract on the Sunn pest, Eurygaste integriceps Puton, growth and development and its gut serine protease activity

The sunn pest Eurygaster integriceps Puton (Hemiptera: Scutelleridae) is a major pest of wheat and barley in wide areas of the world that cause 100% crop loss when no control measures are taken. The aim of this study was to investigate the effect of the seed proteinous extract of different plant species including Chickpea Cicer arietinum (Fabaceae), bean Phaseolus vulgaris var. naz (Fabaceae), triticale Triticosecale wittmack (Poaceae), Celosia argentea (Amaranthaceae) in artificial diet against the Sunn pest growth and development as well as gut serine proteinase such as trypsin and chymotrypsin activities. The obtained results showed that protease inhibitors present in the seed extract affected nymphal development, adult weight and survivability to some extent. Mean developmental time of third and fourth instar nymphs were not significantly affected by the presence of seed extracts. However, developmental time of the fifth instar nymph was affected by seeds proteinous extracts. Bean proteinous extract increased developmental time significantly by almost two days followed by Chickpea that increased developmental time by one day (P < 0.01). Amaranthus seed proteinous extract caused slight increase in development time. Triticale extract did not affect nymph growth and development and there were no significant differences between developmental time of triticale extract and control. Azocaseinolytic activity of gut extract of E. integriceps was affected greatly by seed proteinous extracts. There were significant differences in general protease activity between control and all treatments. General protease activity dropped significantly low when treated with bean and cowpea extracts (P< 0.01). Almost the same trend was observed when trypsin and chymotrypsin activities were measured using BApNA and SAAPFpNA as substrates, respectively. It is concluded that seed extracts from non host plants of the Sunn pest caused significant reduction of general and specific protease activity in vitro.Key words: Sunn pest, growth, development, seed extracts, protease activity

Investigation of the midgut structure and ultrastructure in Cimex lectularius and Cimex pipistrelli (Hemiptera, Cimicidae)

Cimicidae are temporary ectoparasites, which means that they cannot obtain food continuously. Both Cimex species examined here, Cimex lectularius (Linnaeus 1758) and Cimex pipistrelli (Jenyns 1839), can feed on a non-natal host, C. lectularius from humans on bats, C. pipistrelli on humans, but never naturally. The midgut of C. lectularius and C. pipistrelli is composed of three distinct regions—the anterior midgut (AMG), which has a sack-like shape, the long tube-shaped middle midgut (MMG), and the posterior midgut (PMG). The different ultrastructures of the AMG, MMG, and PMG in both of the species examined suggest that these regions must fulfill different functions in the digestive system. Ultrastructural analysis showed that the AMG fulfills the role of storing food and synthesizing and secreting enzymes, while the MMG is the main organ for the synthesis of enzymes, secretion, and the storage of the reserve material. Additionally, both regions, the AMG and MMG, are involved in water absorption in the digestive system of both Cimex species. The PMG is the part of the midgut in which spherites accumulate. The results of our studies confirm the suggestion of former authors that the structure of the digestive tract of insects is not attributed solely to diet but to the basic adaptation of an ancestor

Lipase and invertase activities in midgut and salivary glands of Chilo suppressalis (Walker) (Lepidoptera, Pyralidae), rice striped stem borer

The rice striped stem borer, Chilo supprressalis, was introduced to Iran in 1973 where it is now widely distributed and causes severe damages. Lipases, which catalyses the hydrolysis of fatty acid ester bonds, are widely distributed among animals, plants and microorganisms. Invertases (β-fructofuranosidase) are glycosidehydrolases that catalyze the cleavage of sucrose (β-D-glucopyranosyl-S-D-fructofuranoside) into the monosaccharides glucose and fructose. Laboratory-reared 4th instar larvae were randomly selected, their midgut and salivary glands were removed by dissection under a light microscope and lipase and invertase activities were assayed. The activity of lipase/invertase in the midgut and salivary gland were 0.49/0.27 and 0.35/0.23 μmol/min/mg protein, respectively. The optimum pH and temperature for both the two enzymes were determined to be 10-11 and 37-40 °C, which is consistent with pH and temperature values already observed in Lepidoptera. The enzyme activity was reduced by addition of NaCl, KCl, MgCl2, SDS, urea and plant extracts from Artemisia annua, but not by CaCl2 which enhanced enzyme activity. Pest control with usage of resistant varieties of plants is one of the most important practices that are dependant on inhibitors already present in nature. Hence, characterization of insect digestive enzymes, especially examination of inhibition effects on enzyme activity, could be useful in developing new strategies for pest control

The Amylases of Insects

Alpha-amylases are major digestive enzymes that act in the first step of maltopolysaccharide digestion. In insects, these enzymes have long been studied for applied as well as purely scientific purposes. In many species, amylases are produced by multiple gene copies. Rare species are devoid of Amy gene. They are predominantly secreted in the midgut but salivary expression is also frequent, with extraoral activity. Enzymological parameters are quite variable among insects, with visible trends according to phylogeny: Coleopteran amylases have acidic optimum activity, whereas dipteran amylases have neutral preference and lepidopteran ones have clear alkaline preference. The enzyme structure shows interesting variations shaped by evolutionary convergences, such as the recurrent loss of a loop involved in substrate handling. Many works have focused on the action of plant amylase inhibitors on pest insect amylases, in the frame of crop protection by transgenesis. It appears that sensitivity or resistance to inhibitors is finely tuned and very specific and that amylases and their inhibitors have coevolved. The multicopy feature of insect amylases appears to allow tissue-specific or stage-specific regulation, but also to broaden enzymological abilities, such as pH range, and to overcome plant inhibitory defenses