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Insect Tissues (insect + tissue)
Selected AbstractsGenomic structure and expression analysis of the RNase , family ortholog gene in the insect Ceratitis capitataFEBS JOURNAL, Issue 24 2008Theodoros N. Rampias Cc RNase is the founding member of the recently identified RNase , family, which is represented by a single ortholog in a wide range of animal taxonomic groups. Although the precise biological role of this protein is still unknown, it has been shown that the recombinant proteins isolated so far from the insect Ceratitis capitata and from human exhibit ribonucleolytic activity. In this work, we report the genomic organization and molecular evolution of the RNase , gene from various animal species, as well as expression analysis of the ortholog gene in C. capitata. The high degree of amino acid sequence similarity, in combination with the fact that exon sizes and intronic positions are extremely conserved among RNase , orthologs in 15 diverse genomes from sea anemone to human, imply a very significant biological function for this enzyme. In C. capitata, two forms of RNase , mRNA (0.9 and 1.5 kb) with various lengths of 3, UTR were identified as alternative products of a single gene, resulting from the use of different polyadenylation signals. Both transcripts are expressed in all insect tissues and developmental stages. Sequence analysis of the extended region of the longer transcript revealed the existence of three mRNA instability motifs (AUUUA) and five poly(U) tracts, whose functional importance in RNase , mRNA decay remains to be explored. [source] Spatial distribution and differential expression of the PBAN receptor in tissues of adult Helicoverpa spp. (Lepidoptera: Noctuidae)INSECT MOLECULAR BIOLOGY, Issue 3 2007A. Rafaeli Abstract Pheromone-biosynthesis-activating neuropeptide (PBAN) regulates sex pheromone production in many female moths. PBAN-like peptides, with common FXPRLamide C-terminals are found in other insect groups where they have other functions. The ubiquity and multifunctional nature of the pyrokinin/PBAN family of peptides suggests that the PBAN receptor proteins could also be present in a variety of insect tissues with alternative functions from that of sex pheromone biosynthesis. Previously we showed the presence of the PBAN-R in Helicoverpa armigera at the protein level. In the present study we confirm the similarities between the two Helicoverpa species: armigera and zea by (1) demonstrating the presence of the receptor protein in Sf9 cells, cloned to express the HezPBAN receptor, as compared with the endogenous receptor protein, previously shown in H. armigera pheromone glands, and (2) by identifying the nucleotide sequence of the PBAN-R from mRNA of H. armigera pheromone glands. Sequences of the two Helicoverpa spp. are 98% identical with most changes taking place in the 3,-end. We demonstrate the spatial distribution of the PBAN receptor protein in membranes of H. armigera brain (Br), thoracic ganglion (TG) and ventral nerve cord (VNC). We also demonstrate the presence and differential expression of the PBAN receptor gene (using reverse transcription,polymerase chain reaction and reverse transcription,quantitative real-time polymerase chain reaction, respectively) in the neural tissues (Br, TG and VNC) of adult H. armigera female moths as compared with its presence in pheromone glands. Surprisingly, the gene for the PBAN receptor is also detected in the male tissue homologous to the female pheromone gland, the aedeagus, although the protein is undetectable and PBAN does not induce physiological (pheromone production) or cellular (cyclic-adenosine monophosphate production) responses in this tissue. Our findings indicate that PBAN or PBAN-like receptors are present in the neural tissues and may represent a neurotransmitter-like function for PBAN-like peptides. In addition, the surprising discovery of the presence of the gene encoding the PBAN receptor in the male homologous tissue, but its absence at the protein level, launches opportunities for studying molecular regulation pathways and the evolution of these G protein coupled receptors (GPCRs). [source] Plant-insect interactions: what can we learn from plant lectins?ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 4 2010Katrien Michiels Abstract Many plant lectins have high anti-insect potential. Although the effects of most lectins are only moderately influencing development or population growth of the insect, some lectins have strong insecticidal properties. In addition, some studies report a deterrent activity towards feeding and oviposition behavior. Transmission of plant lectins to the next trophic level has been investigated for several tritrophic interactions. Effects of lectins with different sugar specificities can vary substantially with the insect species under investigation and with the experimental setup. Lectin binding in the insect is an essential step in exerting a toxic effect. Attempts have been made to study the interactions of lectins in several insect tissues and to identify lectin-binding receptors. Ingested lectins generally bind to parts of the insect gut. Furthermore, some lectins such as the Galanthus nivalus agglutinin (GNA) cross the gut epithelium into the hemolymph and other tissues. Recently, several candidate lectin-binding receptors have been isolated from midgut extracts. To date little is known about the exact mechanism for insecticidal activity of plant lectins. However, insect glycobiology is an emerging research field and the recent technological advances in the analysis of lectin carbohydrate specificities and insect glycobiology will certainly lead to new insights in the interactions between plant lectins and insects, and to a better understanding of the molecular mechanisms involved. © 2010 Wiley Periodicals, Inc. [source] Effects of azadirachtin and of simpler epoxy-alcohols on survival and behaviour of Galleria mellonella (Lepidoptera)JOURNAL OF APPLIED ENTOMOLOGY, Issue 7 2007C. Charbonneau Abstract:, Investigations into the toxicity of three simpler molecules based on the epoxy-alcohol fragment of azadirachtin have revealed insecticidal activity on the greater wax moth Galleria mellonella L. larvae. The simpler epoxy-alcohols doses giving 50% mortalities (LD50) for G. mellonella larvae were in the increasing order from glycidol (0.022 mg/g), 4,5-epoxy-2-pentanol (0.068 mg/g) and finally, glycerol diglycidyl ether (0.147 mg/g). The three epoxy-alcohols exhibited higher insecticidal activity when compared with the commercial neem product for which the dose giving 50% mortalities was 10.6 mg/g and to azadirachtin that killed the larvae only by injection (dose of 0.20 mg/g of larvae body weight). Our results confirm the importance of the epoxy-alcohol junction between the two parts of the azadirachtin molecule for the biological activity. Other effects of the epoxy-alcohols tested were blackening of larvae and morphological deformities of some adults hatching. In future, the molecules should be complexified (degree of ramification, length of chain and presence of bulky ramified substituent) to obtain an insecticide as toxic for insects only and environmentally safe as azadirachtin but more stable, and their physiological activities on insect's tissues and cells should be studied. [source] | |||||||||||||