Caddisfly larvae produce silk containing heavy and light fibroins, similar to the silk of Lepidoptera, for the construction of underwater structures. We analyzed the silk of Limnephilus lunatus belonging to the case-forming suborder Integripalpia. We analyzed the transcriptome, mapped the transcripts to a reference genome and identified over 80 proteins using proteomic methods, and checked the specificity of their expression.
View Article and Find Full Text PDFOne of the major functions of the larval salivary glands (SGs) of many Drosophila species is to produce a massive secretion during puparium formation. This so-called proteinaceous glue is exocytosed into the centrally located lumen, and subsequently expectorated, serving as an adhesive to attach the puparial case to a solid substrate during metamorphosis. Although this was first described almost 70 years ago, a detailed description of the morphology and mechanical properties of the glue is largely missing.
View Article and Find Full Text PDFThe grains of durum wheat ( Desf.) and achenes of common buckwheat ( Moench) were tested after treatment with two sources of non-thermal atmospheric pressure plasma (DCSBD, MSDBD) with different treatment times (0, 3, 5, 10, 20, 30, and 40 s). The effect of these treatments was monitored with regard to the seed surface diagnostics (water contact angle-WCA, chemical changes by Fourier transform infrared spectroscopy-FTIR); twenty parameters associated with germination and initial seed growth were monitored.
View Article and Find Full Text PDFComp Biochem Physiol C Toxicol Pharmacol
August 2023
In this study, the biochemical and physiological features of the firebug Pyrrhocoris apterus were investigated to understand the impact of the honeybee Apis mellifera venom on them using physiological methods (mortality, total level of metabolism), biochemical methods (ELISA, mass spectrometry, polyacrylamide gel electrophoresis, spectrophotometry) and molecular methods (real-time PCR). Together, the obtained findings suggest that venom injection increased the level of adipokinetic hormone (AKH) in the CNS of P. apterus, indicating that this hormone plays a key role in activating defence responses.
View Article and Find Full Text PDFSimilar to Lepidoptera, the larvae of Trichoptera are also capable of producing silk. , a predatory species belonging to the suborder Annulipalpia, builds massive silken retreats with preycapturing nets. In this study, we describe the silk glands of and use the multi-omics methods to obtain a complete picture of the fiber composition.
View Article and Find Full Text PDFThe legumes ( family) are the second most important agricultural crop, both in terms of harvested area and total production. They are an important source of vegetable proteins and oils for human consumption. Non-thermal plasma (NTP) treatment is a new and effective method in surface microbial inactivation and seed stimulation useable in the agricultural and food industries.
View Article and Find Full Text PDFMany lepidopteran larvae produce silk feeding shelters and cocoons to protect themselves and the developing pupa. As caterpillars evolved, the quality of the silk, shape of the cocoon, and techniques in forming and leaving the cocoon underwent a number of changes. The silk of has previously been studied using X-ray analysis and classified in the same category as that of , suggesting that silks of both species have similar properties despite their considerable phylogenetic distance.
View Article and Find Full Text PDFLarvae of many lepidopteran species produce a mixture of secretory proteins, known as silk, for building protective shelters and cocoons. Silk consists of a water-insoluble silk filament core produced in the posterior silk gland (PSG) and a sticky hydrophilic coating produced by the middle silk gland (MSG). In Bombyx mori, the fiber core comprises three proteins: heavy chain fibroin (Fib-H), light chain fibroin (Fib-L) and fibrohexamerin (Fhx, previously referred to as P25).
View Article and Find Full Text PDFMany lepidopteran larvae produce silk secretions to build feeding tubes and cocoons that play important protective roles in their lives. Recent research on the silk of bombycoid and pyralid moths has shown that it contains several highly abundant silk components with remarkable mechanical properties. It was also found to contain a number of other proteins of which the functions have yet to be identified.
View Article and Find Full Text PDFComp Biochem Physiol C Toxicol Pharmacol
April 2015
Insect anti-stress responses, including those induced by insecticides, are controlled by adipokinetic hormones (AKHs). We examined the physiological consequences of Pyrap-AKH application on Tribolium castaneum adults (AKH-normal and AKH-deficient prepared by the RNAi technique) treated by two insecticides, pirimiphos-methyl and deltamethrin. Co-application of pirimiphos-methyl and/or deltamethrin with AKH significantly increased beetle mortality compared with application of the insecticides alone.
View Article and Find Full Text PDFArch Insect Biochem Physiol
April 2015
Despite a high toxicity, paraquat is one of the most widely used herbicides in the world. Our study evaluated the effect of paraquat exposure on antioxidant response and locomotion activity in Drosophila melanogaster. We examined the enzymatic activity of superoxide dismutase (SOD) and catalase, and the transcript levels of both enzymes.
View Article and Find Full Text PDFFive neuropeptide genes are classified in the FMRF-related (FaRP) group: the Fmrf, dromyosuppressin (Dms), drosulfakinin (Dsk), neuropeptide F (npf) and short neuropeptide F (sNPF) genes coding for 8, 1, 2, 1 and 4 peptides, respectively. In order to compare their effects on the locomotor activity of Drosophila adults, we made RNAi knockdown of the peptides and their specific receptor genes. In addition, we constructed Gal4 drivers with three distinct parts of the Fmrf gene's 5' regulatory sequence (RS8-Gal4, RS11-Gal4, RS17-Gal4), and used them to ablate FMRF-positive neurons inducing apoptosis by expressing the reaper (rpr) gene.
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